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- PDB-1frt: CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC -

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Basic information

Entry
Database: PDB / ID: 1frt
TitleCRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC
Components
  • BETA 2-MICROGLOBULIN
  • IGG FC
  • NEONATAL FC RECEPTOR
KeywordsCOMPLEX (RECEPTOR/IMMUNOGLOBULIN) / COMPLEX (RECEPTOR-IMMUNOGLOBULIN) / COMPLEX (RECEPTOR-IMMUNOGLOBULIN) complex
Function / homology
Function and homology information


Endosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / IgG receptor activity / IgG binding / Neutrophil degranulation / beta-2-microglobulin binding ...Endosomal/Vacuolar pathway / DAP12 interactions / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / IgG receptor activity / IgG binding / Neutrophil degranulation / beta-2-microglobulin binding / humoral immune response / response to cadmium ion / cellular response to iron ion / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / MHC class II protein complex / negative regulation of forebrain neuron differentiation / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / response to molecule of bacterial origin / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / antigen processing and presentation of exogenous peptide antigen via MHC class II / MHC class I protein complex / positive regulation of immune response / peptide antigen binding / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / positive regulation of receptor-mediated endocytosis / multicellular organismal-level iron ion homeostasis / positive regulation of T cell activation / cellular response to nicotine / positive regulation of cellular senescence / negative regulation of epithelial cell proliferation / MHC class II protein complex binding / late endosome membrane / sensory perception of smell / negative regulation of neuron projection development / iron ion transport / T cell differentiation in thymus / protein refolding / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / endosome membrane / immune response / response to xenobiotic stimulus / external side of plasma membrane / lysosomal membrane / structural molecule activity / protein homodimerization activity / extracellular space / identical protein binding
Similarity search - Function
Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type ...Class I Histocompatibility antigen, domains alpha 1 and 2 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
: / Beta-2-microglobulin / IgG receptor FcRn large subunit p51
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / Resolution: 4.5 Å
AuthorsBurmeister, W.P. / Bjorkman, P.J.
Citation
Journal: Nature / Year: 1994
Title: Crystal structure of the complex of rat neonatal Fc receptor with Fc.
Authors: Burmeister, W.P. / Huber, A.H. / Bjorkman, P.J.
#1: Journal: Nature / Year: 1994
Title: Crystal Structure at 2.2 Angstroms Resolution of the Mhc-Related Neonatal Fc Receptor
Authors: Burmeister, W.P. / Gastinel, L.N. / Simister, N.E. / Blum, M.L. / Bjorkman, P.J.
#2: Journal: Immunity / Year: 1994
Title: Investigation of the Interaction between the Class I Mhc-Related Fc Receptor and its Immunoglobulin G Ligand
Authors: Raghavan, M. / Chen, M.Y. / Gastinel, L.N. / Bjorkman, P.J.
#3: Journal: J.Mol.Biol. / Year: 1993
Title: Crystallization and Stoichiometry of Binding of a Complex between a Rat Intestinal Fc Receptor and Fc
Authors: Huber, A.H. / Kelly, R.F. / Gastinel, L.N. / Bjorkman, P.J.
#4: Journal: Biochemistry / Year: 1981
Title: Crystallographic Refinement and Atomic Models of a Human Fc Fragment and its Complex with Fragment B of Protein a from Staphylococcus Aureus at 2.9-And 2.8-Angstroms Resolution
Authors: Deisenhofer, J.
History
DepositionNov 11, 1994Processing site: BNL
Revision 1.0Feb 14, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.3Feb 5, 2020Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Other
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif
Item: _chem_comp.type / _pdbx_database_status.process_site ..._chem_comp.type / _pdbx_database_status.process_site / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.oper_expression / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / pdbx_validate_symm_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _database_PDB_caveat.text / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_symm_contact.auth_asym_id_2 / _pdbx_validate_symm_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 25, 2024Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_validate_symm_contact / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: NEONATAL FC RECEPTOR
B: BETA 2-MICROGLOBULIN
C: IGG FC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,6126
Polymers65,3983
Non-polymers2,2143
Water00
1
A: NEONATAL FC RECEPTOR
B: BETA 2-MICROGLOBULIN
C: IGG FC
hetero molecules

A: NEONATAL FC RECEPTOR
B: BETA 2-MICROGLOBULIN
C: IGG FC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)135,22412
Polymers130,7956
Non-polymers4,4286
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_565x,-y+1,-z+1/21
Unit cell
Length a, b, c (Å)125.000, 145.000, 216.500
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Space group name H-MI212121
Atom site foot note1: CIS PROLINE - PRO A 207 / 2: CIS PROLINE - PRO B 32 / 3: CIS PROLINE - PRO C 374
DetailsMTRIX THE INFORMATION PRESENTED ON SYMMETRY RECORDS BELOW DESCRIBE TRANSFORMATIONS TO GENERATE CRYSTALLOGRAPHIC RELATIONSHIPS AS DESCRIBED IN THE STATEMENT THAT FOLLOWS EACH SYMMETRY OPERATOR. APPLIED TO TRANSFORMED TO MTRIX CHAIN RESIDUES CHAIN RESIDUES RMSD S1 C 1 - C 443 ? 1 - ? 443 THIS TRANSFORMATION GENERATES THE SECOND CHAIN OF THE FC MOLECULE. IF THE SAME OPERATION IS ALSO APPLIED TO THE FCRN MOLECULE, THE "STANDING UP" FCRNFC COMPLEX DISCUSSED IN THE ACCOMPANYING PAPER IS GENERATED. S2 A 1 - A 405 ? 1 - ? 405 S2 B 1 - B 99 ? 1 - ? 99 THIS TRANSFORMATION GENERATES THE SECOND SUBUNIT FOR THE "LYING DOWN" FC RECEPTOR DIMER PRESENTED IN THE ACCOMPANYING PAPER. SYMMETRY1 1 1.000000 0.000000 0.000000 0.00000 SYMMETRY2 1 0.000000 -1.000000 0.000000 145.00000 SYMMETRY3 1 0.000000 0.000000 -1.000000 108.25000 SYMMETRY1 2 -1.000000 0.000000 0.000000 250.00000 SYMMETRY2 2 0.000000 -1.000000 0.000000 72.50000 SYMMETRY3 2 0.000000 0.000000 1.000000 0.00000

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein NEONATAL FC RECEPTOR


Mass: 30322.887 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: BETA-2-MICROGLOBULIN / Organ: SERUM (MIXTURE OF SEVERAL SUBTYPES) / Plasmid: PBJ5-GS / Cell line (production host): CHO / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P13599
#2: Protein BETA 2-MICROGLOBULIN


Mass: 11652.282 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: BETA-2-MICROGLOBULIN / Organ: SERUM (MIXTURE OF SEVERAL SUBTYPES) / Plasmid: PBJ5-GS / Cell line (production host): CHO / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P07151
#3: Protein IGG FC


Mass: 23422.539 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: BETA-2-MICROGLOBULIN / Organ: SERUM (MIXTURE OF SEVERAL SUBTYPES) / Plasmid: PBJ5-GS / Cell line (production host): CHO / Production host: Cricetulus griseus (Chinese hamster) / References: GenBank: 243866

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Sugars , 3 types, 3 molecules

#4: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose- ...beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1625.490 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGalpb1-4DGlcpNAcb1-2DManpa1-6[DGlcpNAcb1-2DManpa1-3]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/5,9,8/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a2112h-1b_1-5][a1221m-1a_1-5]/1-1-2-3-1-3-1-4-5/a4-b1_a6-i1_b4-c1_c3-d1_c6-f1_d2-e1_f2-g1_g4-h1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{}}}}}[(6+1)][a-D-6-deoxy-Altp]{}}}LINUCSPDB-CARE
#6: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Details

Has protein modificationY
Sequence detailsTHERE ARE A NUMBER OF CLOSE CONTACTS BETWEEN ATOMS IN THIS THIS MOLECULE AND IN SYMMETRY-RELATED MOLECULES.
Source detailsSOURCE 1 MOLECULE_NAME: FC (IGG) RECEPTOR, NEONATAL (FCRN) THE CELL LINE SECRETES A SOLUBLE FCRN ...SOURCE 1 MOLECULE_NAME: FC (IGG) RECEPTOR, NEONATAL (FCRN) THE CELL LINE SECRETES A SOLUBLE FCRN HETERODIMER COMPOSED OF THE EXTRACELLULAR DOMAINS OF THE RAT FCRN HEAVY CHAIN ASSOCIATED WITH RAT BETA-2-MICROGLOBULIN. SOURCE 2 MOLECULE_NAME: FC FRAGMENT (IGG) OBTAINED FROM JACKSON IMMUNORESEARCH LABS. THE FC FRAGMENT IS A MIXTURE OF SUBTYPES 1, 2A, 2B, AND 2C. THE N-TERMINUS IS NOT PRECISELY KNOWN, BUT THE CLEAVAGE SITE IS C-TERMINAL TO THE DISULFIDE BONDS OF THE HINGE REGION. THE FRAGMENT IS, THEREFORE, A NON-COVALENT DIMER.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

Crystal grow
*PLUS
pH: 6.4 / Method: vapor diffusion
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
115 mg/mlprotein1drop
210 mMPIPES1drop
30.05 %1dropNaN3
40.67 Msodium tartarate1reservoir
5100 mMcitrate1reservoir

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionNum. obs: 8527 / % possible obs: 67 % / Observed criterion σ(I): 0
Reflection
*PLUS
Highest resolution: 4.5 Å / Lowest resolution: 25 Å / Redundancy: 3 % / Rmerge(I) obs: 0.125
Reflection shell
*PLUS
Highest resolution: 4.5 Å / Lowest resolution: 4.7 Å / % possible obs: 23 % / Rmerge(I) obs: 0.289

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
RefinementResolution: 4.5→20 Å / σ(F): 0
RfactorNum. reflection% reflection
Rwork0.423 --
obs0.423 8433 67 %
Displacement parametersBiso mean: 199 Å2
Refinement stepCycle: LAST / Resolution: 4.5→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4608 0 148 0 4756

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