1f8a
From Proteopedia
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- | [[Image:1f8a.gif|left|200px]] | + | [[Image:1f8a.gif|left|200px]] |
- | + | ||
- | '''STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS''' | + | {{Structure |
+ | |PDB= 1f8a |SIZE=350|CAPTION= <scene name='initialview01'>1f8a</scene>, resolution 1.84Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITION BY GROUP IV WW DOMAINS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1F8A is a [ | + | 1F8A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F8A OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10932246 10932246] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[Category: ww domain]] | [[Category: ww domain]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:44 2008'' |
Revision as of 09:05, 20 March 2008
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, resolution 1.84Å | |||||||
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Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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