1F8A

STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS

Summary for 1F8A

• Entry DOI: 10.2210/pdb1f8a/pdb
• Related: 1PIN
• Descriptor: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1, Y(SEP)PT(SEP)S PEPTIDE (3 entities in total)
• Functional Keywords: peptidyl-proline isomerase, ww domain, phosphoserine binding, isomerase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q13526
• Total number of polymer chains: 2
• Total formula weight: 19508.35

Authors

Verdecia, M.A.,Bowman, M.E.,Lu, K.P.,Hunter, T.,Noel, J.P. (deposition date: 2000-06-29, release date: 2000-08-23, Last modification date: 2024-10-16)

Primary citation

Verdecia, M.A.,Bowman, M.E.,Lu, K.P.,Hunter, T.,Noel, J.P.
Structural basis for phosphoserine-proline recognition by group IV WW domains.
Nat.Struct.Biol., 7:639-643, 2000

PubMed Abstract: 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.

PubMed: 10932246
DOI: 10.1038/77929

Experimental method

X-RAY DIFFRACTION (1.84 Å)