3NH7

Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.236 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

A selection fit mechanism in BMP receptor IA as a possible source for BMP ligand-receptor promiscuity

Harth, S., Kotzsch, A., Hu, J., Sebald, W., Mueller, T.D.

(2010) PLoS One 5: e13049-e13049

  • DOI: https://doi.org/10.1371/journal.pone.0013049
  • Primary Citation of Related Structures:  
    3NH7

  • PubMed Abstract: 

    Members of the TGF-β superfamily are characterized by a highly promiscuous ligand-receptor interaction as is readily apparent from the numeral discrepancy of only seven type I and five type II receptors available for more than 40 ligands. Structural and functional studies have been used to address the question of how specific signals can be deduced from a limited number of receptor combinations and to unravel the molecular mechanisms underlying the protein-protein recognition that allow such limited specificity.

    • Organizational Affiliation: 

    Lehrstuhl für Physiologische Chemie II, Theodor-Boveri-Institut für Biowissenschaften der Universität Würzburg, Würzburg, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Antibody fragment Fab AbD1556, heavy chainA [auth H],
D [auth I],
G [auth J],
J [auth K]		234Homo sapiensMutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Antibody fragment Fab AbD1556, light chainB [auth L],
E [auth M],
H [auth N],
K [auth O]		213Homo sapiensMutation(s): 0 
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Bone morphogenetic protein receptor type-1AC [auth A],
F [auth B],
I [auth C],
L [auth D]		129Homo sapiensMutation(s): 0 
Gene Names: BMPR1A
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 
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UniProt GroupP36894
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.234 
  • R-Value Observed: 0.236 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 89.32α = 90
b = 129.255β = 92.27
c = 100.239γ = 90
Software Package:
Software NamePurpose
CrystalCleardata collection
PHASERphasing
REFMACrefinement
CrystalCleardata reduction
CrystalCleardata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-10-27
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-11-01
    Changes: Data collection, Database references, Refinement description