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An autonomously folding β‐hairpin derived from the human YAP65 WW domain: Attempts to define a minimum ligand‐binding motif
Author(s) -
Espinosa Juan F.,
Syud Faisal A.,
Gellman Samuel H.
Publication year - 2005
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20205
Subject(s) - ww domain , chemistry , beta sheet , folding (dsp implementation) , ligand (biochemistry) , crystallography , biophysics , protein folding , stereochemistry , peptide , biochemistry , receptor , biology , electrical engineering , gene , engineering
WW domains are broadly distributed among natural proteins; these modules play a role in bringing specific proteins together. The ligands recognized by WW domains are short segments rich in proline residues. We have tried to identify the minimum substructure within a WW domain that is required for ligand binding. WW domains typically comprise ca. 40 residues and fold to a three‐stranded β‐sheet. Structural data for several WW domain/ligand complexes suggest that most or all of the intermolecular contacts involve β‐strands 2 and 3. We have developed a 16‐residue peptide that folds to a β‐hairpin conformation that appears to mimic β‐strands 2 and 3 of the human YAP65 WW domain, but this peptide does not bind to known ligands. Thus, the minimum binding domain is larger than the latter two strands of the WW domain β‐sheet. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005