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- PDB-3mzg: Crystal structure of a human prolactin receptor antagonist in com... -

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Basic information

Entry
Database: PDB / ID: 3mzg
TitleCrystal structure of a human prolactin receptor antagonist in complex with the extracellular domain of the human prolactin receptor
Components
  • Prolactin
  • Prolactin receptor
KeywordsHORMONE/HORMONE RECEPTOR / ECD / antagonist / pH dependence / hematopoietic cytokine / HORMONE-HORMONE RECEPTOR complex
Function / homology
Function and homology information


prolactin receptor activity / prolactin receptor binding / activation of transmembrane receptor protein tyrosine kinase activity / positive regulation of lactation / regulation of epithelial cell differentiation / prolactin signaling pathway / mammary gland epithelial cell differentiation / activation of Janus kinase activity / steroid biosynthetic process / prostate gland growth ...prolactin receptor activity / prolactin receptor binding / activation of transmembrane receptor protein tyrosine kinase activity / positive regulation of lactation / regulation of epithelial cell differentiation / prolactin signaling pathway / mammary gland epithelial cell differentiation / activation of Janus kinase activity / steroid biosynthetic process / prostate gland growth / cellular response to granulocyte macrophage colony-stimulating factor stimulus / mammary gland development / Prolactin receptor signaling / cytokine binding / negative regulation of endothelial cell proliferation / peptide hormone binding / mammary gland alveolus development / cell surface receptor signaling pathway via JAK-STAT / Growth hormone receptor signaling / regulation of cell adhesion / lactation / positive regulation of B cell proliferation / embryo implantation / negative regulation of angiogenesis / endosome lumen / positive regulation of receptor signaling pathway via JAK-STAT / response to bacterium / response to nutrient levels / female pregnancy / hormone activity / positive regulation of miRNA transcription / cytokine-mediated signaling pathway / positive regulation of cold-induced thermogenesis / cell surface receptor signaling pathway / positive regulation of canonical NF-kappaB signal transduction / receptor complex / Amyloid fiber formation / external side of plasma membrane / positive regulation of cell population proliferation / lipid binding / protein kinase binding / negative regulation of apoptotic process / cell surface / extracellular space / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
Somatotropin/prolactin / Somatotropin hormone, conserved site / Somatotropin hormone family / Somatotropin, prolactin and related hormones signature 1. / Somatotropin, prolactin and related hormones signature 2. / Long hematopoietin receptor, single chain, conserved site / Growth hormone/erythropoietin receptor, ligand binding / Erythropoietin receptor, ligand binding / Long hematopoietin receptor, single chain family signature. / : ...Somatotropin/prolactin / Somatotropin hormone, conserved site / Somatotropin hormone family / Somatotropin, prolactin and related hormones signature 1. / Somatotropin, prolactin and related hormones signature 2. / Long hematopoietin receptor, single chain, conserved site / Growth hormone/erythropoietin receptor, ligand binding / Erythropoietin receptor, ligand binding / Long hematopoietin receptor, single chain family signature. / : / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Prolactin / Prolactin receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsKulkarni, M.V. / Tettamanzi, M.C. / Murphy, J.W. / Keeler, C. / Myszka, D.G. / Chayen, N.E. / Lolis, E.J. / Hodsdon, M.E.
CitationJournal: J.Biol.Chem. / Year: 2010
Title: Two Independent Histidines, One in Human Prolactin and One in Its Receptor, Are Critical for pH-dependent Receptor Recognition and Activation.
Authors: Kulkarni, M.V. / Tettamanzi, M.C. / Murphy, J.W. / Keeler, C. / Myszka, D.G. / Chayen, N.E. / Lolis, E.J. / Hodsdon, M.E.
History
DepositionMay 12, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 29, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _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.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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Prolactin
B: Prolactin receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,3426
Polymers46,2382
Non-polymers1044
Water4,738263
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2940 Å2
ΔGint-49 kcal/mol
Surface area19950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)123.874, 123.874, 72.468
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65

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Components

#1: Protein Prolactin / PRL


Mass: 21791.883 Da / Num. of mol.: 1 / Fragment: sequence database residues 43-227
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRL, Prolactin / Plasmid: pT7L-hPRL-del1-14-G129R / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P01236
#2: Protein Prolactin receptor / PRL-R


Mass: 24445.840 Da / Num. of mol.: 1 / Fragment: Extracellular domain residues 26-234
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PRLR, Prolactin receptor / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P16471
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 263 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.47 Å3/Da / Density % sol: 64.57 %
Crystal growTemperature: 291 K / pH: 7.5
Details: 3.7 M NaCl; 0.1M Hepes pH 7.5, 600nL + 100 nL drops, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.0809
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 13, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0809 Å / Relative weight: 1
ReflectionResolution: 2→33 Å / Num. obs: 40530 / % possible obs: 94 % / Observed criterion σ(I): 1 / Redundancy: 9.5 % / Rsym value: 0.082 / Net I/σ(I): 23.1
Reflection shellResolution: 2→2.07 Å / Redundancy: 9.1 % / Mean I/σ(I) obs: 3.7 / Rsym value: 0.601 / % possible all: 99.3

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Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
REFMAC5.5.0109refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: CHIMERA OF PDB ENTRIES 3D48, 2Q98, AND 1BP3

3d48

2q98

1bp3


Resolution: 2.1→32.07 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.935 / SU B: 4.124 / SU ML: 0.11 / Cross valid method: THROUGHOUT / ESU R: 0.164 / ESU R Free: 0.156 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.22975 1867 5.1 %RANDOM
Rwork0.18672 ---
obs0.1889 34830 98.96 %-
all-43123 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.708 Å2
Baniso -1Baniso -2Baniso -3
1--2.03 Å2-1.01 Å20 Å2
2---2.03 Å20 Å2
3---3.04 Å2
Refinement stepCycle: LAST / Resolution: 2.1→32.07 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3209 0 4 263 3476
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0250.0223343
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.0911.9534555
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.7985404
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.08924.088159
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.94115580
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.5351518
X-RAY DIFFRACTIONr_chiral_restr0.1550.2484
X-RAY DIFFRACTIONr_gen_planes_refined0.0120.0212564
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.4881.51990
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.6923248
X-RAY DIFFRACTIONr_scbond_it3.83831353
X-RAY DIFFRACTIONr_scangle_it6.1994.51300
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.241 148 -
Rwork0.206 2546 -
obs--99.26 %

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