1YWI

Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP

Summary for 1YWI

• Entry DOI: 10.2210/pdb1ywi/pdb
• Related: 1CKA 1EG4 1F8A 1I5H 1YWJ 1o6w
• NMR Information: BMRB: 6559
• Descriptor: Formin-binding protein 3, Formin (2 entities in total)
• Functional Keywords: ww domain, class ii, proline-rich peptides, protein-protein interactions, structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus speckle (By similarity): O75400
• Total number of polymer chains: 2
• Total formula weight: 5730.25

Authors

Pires, J.R.,Parthier, C.,Aido-Machado, R.,Wiedemann, U.,Otte, L.,Boehm, G.,Rudolph, R.,Oschkinat, H. (deposition date: 2005-02-18, release date: 2005-04-12, Last modification date: 2024-05-29)

Primary citation

Pires, J.R.,Parthier, C.,Aido-Machado, R.,Wiedemann, U.,Otte, L.,Bohm, G.,Rudolph, R.,Oschkinat, H.
Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.
J.Mol.Biol., 348:399-408, 2005

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.

PubMed: 15811376
DOI: 10.1016/j.jmb.2005.02.056

Experimental method

SOLUTION NMR