1A4P

P11 (S100A10), LIGAND OF ANNEXIN II


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.246 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

The crystal structure of a complex of p11 with the annexin II N-terminal peptide.

Rety, S.Sopkova, J.Renouard, M.Osterloh, D.Gerke, V.Tabaries, S.Russo-Marie, F.Lewit-Bentley, A.

(1999) Nat Struct Biol 6: 89-95

  • DOI: https://doi.org/10.1038/4965
  • Primary Citation of Related Structures:  
    1A4P, 1BT6

  • PubMed Abstract: 

    The aggregation and membrane fusion properties of annexin II are modulated by the association with a regulatory light chain called p11.p11 is a member of the S100 EF-hand protein family, which is unique in having lost its calcium-binding properties. We report the first structure of a complex between p11 and its cognate peptide, the N-terminus of annexin II, as well as that of p11 alone. The basic unit for p11 is a tight, non-covalent dimer. In the complex, each annexin II peptide forms hydrophobic interactions with both p11 monomers, thus providing a structural basis for high affinity interactions between an S100 protein and its target sequence. Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.


  • Organizational Affiliation

    LURE (CNRS, CEA, MENRT), Centre Universitaire Paris-Sud, Orsay, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
S100A10
A, B
96Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P60903 (Homo sapiens)
Explore P60903 
Go to UniProtKB:  P60903
PHAROS:  P60903
GTEx:  ENSG00000197747 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP60903
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.246 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 57.75α = 90
b = 80.75β = 90
c = 95.51γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
REFMACrefinement

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-05-27
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance