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1pin

From Proteopedia

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[[Image:1pin.gif|left|200px]]
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{{STRUCTURE_1pin| PDB=1pin | SCENE= }}
{{STRUCTURE_1pin| PDB=1pin | SCENE= }}
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'''PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS'''
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===PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS===
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==Overview==
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The human rotamase or peptidyl-prolyl cis-trans isomerase Pin1 is a conserved mitotic regulator essential for the G2/M transition of the eukaryotic cell cycle. We report the 1.35 A crystal structure of Pin1 complexed with an AlaPro dipeptide and the initial characterization of Pin1's functional properties. The crystallographic structure as well as pH titration studies and mutagenesis of an active site cysteine suggest a catalytic mechanism that includes general acid-base and covalent catalysis during peptide bond isomerization. Pin1 displays a preference for an acidic residue N-terminal to the isomerized proline bond due to interaction of this acidic side chain with a basic cluster. This raises the possibility of phosphorylation-mediated control of Pin1-substrate interactions in cell cycle regulation.
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==About this Structure==
==About this Structure==
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[[Category: Peptidyl-prolyl cis-trans isomerase]]
[[Category: Peptidyl-prolyl cis-trans isomerase]]
[[Category: Rotamase]]
[[Category: Rotamase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:50:08 2008''

Revision as of 11:50, 28 July 2008

Image:1pin.png

Template:STRUCTURE 1pin

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

Template:ABSTRACT PUBMED 9200606

About this Structure

1PIN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent., Ranganathan R, Lu KP, Hunter T, Noel JP, Cell. 1997 Jun 13;89(6):875-86. PMID:9200606

Page seeded by OCA on Mon Jul 28 14:50:08 2008

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