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- PDB-1jc7: The Laminin-Binding Domain of Agrin is Structurally Related to N-... -

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Basic information

Entry
Database: PDB / ID: 1jc7
TitleThe Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1
ComponentsAgrin
KeywordsCELL ADHESION / NEUROMUSCULAR JUNCTION / AGRIN / INTERACTION COILED-DOIL PROTEINS WITH GLOBULAR PROTEINS / OB-FOLD / TIMP
Function / homology
Function and homology information


acetylcholine receptor regulator activity / extracellular matrix of synaptic cleft / positive regulation of synaptic assembly at neuromuscular junction / chondroitin sulfate binding / skeletal muscle acetylcholine-gated channel clustering / laminin-1 binding / sialic acid binding / photoreceptor ribbon synapse / neuron cell-cell adhesion / dystroglycan binding ...acetylcholine receptor regulator activity / extracellular matrix of synaptic cleft / positive regulation of synaptic assembly at neuromuscular junction / chondroitin sulfate binding / skeletal muscle acetylcholine-gated channel clustering / laminin-1 binding / sialic acid binding / photoreceptor ribbon synapse / neuron cell-cell adhesion / dystroglycan binding / basal part of cell / filopodium assembly / transmembrane receptor protein tyrosine kinase activator activity / glycosaminoglycan binding / heparan sulfate proteoglycan binding / extracellular matrix binding / positive regulation of filopodium assembly / neuromuscular junction development / receptor clustering / basement membrane / positive regulation of GTPase activity / laminin binding / extracellular matrix / neuromuscular junction / brain development / nervous system development / signaling receptor activity / heparin binding / negative regulation of neuron projection development / actin cytoskeleton organization / cell differentiation / membrane raft / axon / calcium ion binding / synapse / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / plasma membrane
Similarity search - Function
NtA (N-terminal agrin) domain / Agrin NtA domain / NtA (N-terminal agrin) domain profile. / Follistatin-like, N-terminal / Follistatin-N-terminal domain-like / Factor I / membrane attack complex / factor I membrane attack complex / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / Laminin G domain / Laminin-type EGF-like (LE) domain profile. ...NtA (N-terminal agrin) domain / Agrin NtA domain / NtA (N-terminal agrin) domain profile. / Follistatin-like, N-terminal / Follistatin-N-terminal domain-like / Factor I / membrane attack complex / factor I membrane attack complex / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / Laminin G domain / Laminin-type EGF-like (LE) domain profile. / Laminin-type EGF-like (LE) domain signature. / Laminin-type epidermal growth factor-like domai / Laminin EGF domain / Domain found in sea urchin sperm protein, enterokinase, agrin / : / Laminin-type EGF domain / SEA domain superfamily / Kazal-type serine protease inhibitor domain / Kazal-type serine protease inhibitor domain / SEA domain profile. / SEA domain / SEA domain / Kazal type serine protease inhibitors / Laminin G domain profile. / Laminin G domain / Laminin G domain / Kazal domain superfamily / Kazal domain / Kazal domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Concanavalin A-like lectin/glucanase domain superfamily / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.73 Å
AuthorsStetefeld, J.
CitationJournal: Nat.Struct.Biol. / Year: 2001
Title: The laminin-binding domain of agrin is structurally related to N-TIMP-1.
Authors: Stetefeld, J. / Jenny, M. / Schulthess, T. / Landwehr, R. / Schumacher, B. / Frank, S. / Ruegg, M.A. / Engel, J. / Kammerer, R.A.
History
DepositionJun 8, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 8, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 30, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_source / pdbx_entry_details / pdbx_modification_feature / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Agrin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)15,1832
Polymers15,1471
Non-polymers351
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)85.306, 49.899, 54.328
Angle α, β, γ (deg.)90.00, 118.43, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Agrin


Mass: 15147.343 Da / Num. of mol.: 1 / Fragment: LAMININ-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Production host: Escherichia coli (E. coli) / References: UniProt: Q90685, UniProt: P31696*PLUS
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
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: 3.36 Å3/Da / Density % sol: 63.34 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.8
Details: PEG4000, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Crystal grow
*PLUS
Temperature: 4 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
18 mg/mlprotein1drop
20.1 Mcitrate1drop
30.1 Mcitrate1reservoir
420 %(w/v)PEG40001reservoir
510 %(w/v)2-propanol1reservoir
610 %(w/v)MPD1reservoir

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.847 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.847 Å / Relative weight: 1
ReflectionBiso Wilson estimate: 26.4 Å2
Reflection
*PLUS
Highest resolution: 2.7 Å / % possible obs: 99.1 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.086
Reflection shell
*PLUS
% possible obs: 94.3 % / Rmerge(I) obs: 0.272

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
CNS1refinement
CCP4(SCALA)data scaling
RefinementResolution: 2.73→27.92 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 664563.5 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT
RfactorNum. reflection% reflectionSelection details
Rfree0.249 539 10.4 %RANDOM
Rwork0.207 ---
obs0.207 5189 95.1 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 24.06 Å2 / ksol: 0.304 e/Å3
Displacement parametersBiso mean: 35.9 Å2
Baniso -1Baniso -2Baniso -3
1-4.93 Å20 Å2-0.07 Å2
2--3.46 Å20 Å2
3----8.39 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.43 Å0.34 Å
Luzzati d res low-30 Å
Luzzati sigma a0.39 Å0.32 Å
Refinement stepCycle: LAST / Resolution: 2.73→27.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1046 0 1 0 1047
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.007
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d23.9
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.72
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 2.7→2.87 Å / Rfactor Rfree error: 0.05 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.342 47 9.3 %
Rwork0.316 459 -
obs--54.8 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMION.TOP
X-RAY DIFFRACTION3ION.PARAMWATER.TOP
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refinement
*PLUS
% reflection Rfree: 10.4 %
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 35.9 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.3
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg23.9
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.72
LS refinement shell
*PLUS
Rfactor Rfree: 0.342 / % reflection Rfree: 9.3 % / Rfactor Rwork: 0.316

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