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1f8a
From Proteopedia
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STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS
Overview
Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl, cis-trans isomerase (PPIase) domain connected by a flexible linker. To, address the energetic and structural basis for WW domain recognition of, phosphoserine (P.Ser)/phosphothreonine (P. Thr)- proline containing, proteins, we report the energetic and structural analysis of a, Pin1-phosphopeptide complex. The X-ray crystal structure of Pin1 bound to, a doubly phosphorylated peptide (Tyr-P.Ser-Pro-Thr-P.Ser-Pro-Ser), representing a heptad repeat of the RNA polymerase II large subunit's, C-terminal domain (CTD), reveals the residues involved in the recognition, of a single P.Ser side chain, the rings of two prolines, and the backbone, of the CTD peptide. The side chains of neighboring Arg and Ser residues, along with a backbone amide contribute to recognition of P.Ser. The lack, of widespread conservation of the Arg and Ser residues responsible for, P.Ser recognition in the WW domain family suggests that only a subset of, WW domains can bind P.Ser-Pro in a similar fashion to that of Pin1.
About this Structure
1F8A is a Single protein structure of sequence from Homo sapiens. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
Reference
Structural basis for phosphoserine-proline recognition by group IV WW domains., Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP, Nat Struct Biol. 2000 Aug;7(8):639-43. PMID:10932246
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