PDBsum entry 1ywi

Structural protein

PDB id: 1ywi

Contents

Protein chain

28 a.a. *

Ligands

PRO-PRO-PRO-LEU-PRO-PRO

* Residue conservation analysis

PDB id:

1ywi

Name:

Structural protein

Title:

Structure of the fbp11ww1 domain complexed to the peptide apptppplpp

Structure:

Formin-binding protein 3. Chain: a. Fragment: ww1 domain. Synonym: formin binding protein 11. Engineered: yes. Formin. Chain: b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: automated solid phase synthesis on chlortrityl resin using fmoc strategy

NMR struc:

15 models

Authors:

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

Key ref:

J.R.Pires et al. (2005). Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain. J Mol Biol, 348, 399-408. PubMed id: 15811376 DOI: 10.1016/j.jmb.2005.02.056

Date:

18-Feb-05 Release date: 12-Apr-05

Protein chain

O75400  (PR40A_HUMAN) -  Pre-mRNA-processing factor 40 homolog A from Homo sapiens

Seq: 957 a.a.

Struc: 28 a.a.

DOI no: 10.1016/j.jmb.2005.02.056

J Mol Biol 348:399-408 (2005)

PubMed id: 15811376

Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain.

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

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.

Selected figure(s)

Figure 1.
Figure 1. The WW domain sequences and classes. Amino acid sequence of selected WW domains grouped in classes according to ligand specificity.4 Classes/ligand motifs: class II PPLPp (magenta), class III (p/ )P(p/g)PPpR or (p/ )PPRgpPp (orange), class IV (poS/poT)P (green) and class I PPxY (blue). Conserved amino acid residues are in bold; amino acid residues on the b-strand face where binding occurs are grey-shaded; amino acid residues responsible for class specificity are colored. The asterisk (*) indicates sequences assumed to be FBP11 orthologs.

Figure 4.
Figure 4. Comparison of WW and SH3 domain complexes. (a) Schematic representation of a WW domain showing important regions for ligand recognition. Residues conserved for all WW domains are displayed in blue. Positions changing between the WW domain specificity classes are shown in green, next to which the amino acid types and their corresponding WW domain classes are indicated in parentheses. Superposition of FBP11WW1 (grey ribbon, blue side-chains, class II) complexed to APPTPPPLPP (cyan) with: (b) dystrophinWW domain (red, class I) in complex with SPPPY (yellow); (c) Pin1WW domain (red, class IV): in complex with (poS)PT(poS)PS (yellow); and (d) the C-CRK N-terminal SH3 domain (red) in complex with PPPALPPK (yellow). (e) PRP40WW1 (red, class II) and (f) PRP40WW2 (red, class II)

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 348, 399-408) copyright 2005.

Figures were selected by an automated process.