1YWJ

Structure of the FBP11WW1 domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.

Pires, J.R.Parthier, C.Aido-Machado, R.Wiedemann, U.Otte, L.Bohm, G.Rudolph, R.Oschkinat, H.

(2005) J Mol Biol 348: 399-408

  • DOI: https://doi.org/10.1016/j.jmb.2005.02.056
  • Primary Citation of Related Structures:  
    1YWI, 1YWJ

  • PubMed Abstract: 

    WW domains are small protein-protein interaction modules that recognize proline-rich stretches in proteins. The class II tandem WW domains of the formin binding protein 11 (FBP11) recognize specifically proteins containing PPLPp motifs as present in the formins that are involved in limb and kidney development, and in the methyl-CpG-binding protein 2 (MeCP2), associated with the Rett syndrome. The interaction involves the specific recognition of a leucine side-chain. Here, we report on the novel structure of the complex formed by the FPB11WW1 domain and the formin fragment APPTPPPLPP revealing the specificity determinants of class II WW domains.


  • Organizational Affiliation

    Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, Av. Brigadeiro Trompowiski s/n CCS, Rio de Janeiro, RJ 21941-590, Brazil. jrmpires@gmx.net


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Formin-binding protein 341Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O75400 (Homo sapiens)
Explore O75400 
Go to UniProtKB:  O75400
PHAROS:  O75400
GTEx:  ENSG00000196504 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO75400
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-04-12
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Data collection, Database references, Derived calculations
  • Version 1.4: 2024-05-29
    Changes: Data collection