2H64

Crystal structure of a ternary ligand-receptor complex of BMP-2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.92 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.232 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A silent H-bond can be mutationally activated for high-affinity interaction of BMP-2 and activin type IIB receptor.

Weber, D.Kotzsch, A.Nickel, J.Harth, S.Seher, A.Mueller, U.Sebald, W.Mueller, T.D.

(2007) BMC Struct Biol 7: 6-6

  • DOI: https://doi.org/10.1186/1472-6807-7-6
  • Primary Citation of Related Structures:  
    2H62, 2H64

  • PubMed Abstract: 

    Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as high-affinity receptors for activins but are also low-affinity receptors for BMPs. ActR-II and ActR-IIB therefore represent an interesting example how affinity and specificity might be generated in a promiscuous background.


  • Organizational Affiliation

    Lehrstuhl für Physiologische Chemie II, Theodor-Boveri Institut für Biowissenschaften (Biozentrum) der Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany. dweber@biozentrum.uni-wuerzburg.de


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bone morphogenetic protein 2114Homo sapiensMutation(s): 2 
Gene Names: BMP2BMP2A
UniProt & NIH Common Fund Data Resources
Find proteins for P12643 (Homo sapiens)
Explore P12643 
Go to UniProtKB:  P12643
PHAROS:  P12643
GTEx:  ENSG00000125845 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP12643
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Bone morphogenetic protein receptor type IA129Homo sapiensMutation(s): 0 
Gene Names: BMPR1AACVRLK3ALK3
EC: 2.7.11.30
UniProt & NIH Common Fund Data Resources
Find proteins for P36894 (Homo sapiens)
Explore P36894 
Go to UniProtKB:  P36894
PHAROS:  P36894
GTEx:  ENSG00000107779 
Entity Groups  
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UniProt GroupP36894
Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Acvr2b protein99Mus musculusMutation(s): 0 
Gene Names: Acvr2b
UniProt & NIH Common Fund Data Resources
Find proteins for P27040 (Mus musculus)
Explore P27040 
Go to UniProtKB:  P27040
IMPC:  MGI:87912
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP27040
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.92 Å
  • R-Value Free: 0.264 
  • R-Value Work: 0.228 
  • R-Value Observed: 0.232 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 82.79α = 90
b = 82.79β = 90
c = 111.12γ = 120
Software Package:
Software NamePurpose
CrystalCleardata collection
d*TREKdata reduction
PHASERphasing
CNSrefinement
CrystalCleardata reduction
d*TREKdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-04-10
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-20
    Changes: Database references