1pin: Difference between revisions
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[[Image:1pin.gif|left|200px]]<br /><applet load="1pin" size=" | [[Image:1pin.gif|left|200px]]<br /><applet load="1pin" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pin, resolution 1.35Å" /> | caption="1pin, resolution 1.35Å" /> | ||
'''PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS'''<br /> | '''PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1PIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and 1PG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=ACT:The Active Site Of Ppiase Domain Is Marked By The Bound ...'>ACT</scene>. Full crystallographic information is available from [http:// | 1PIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=1PG:'>1PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=ACT:The+Active+Site+Of+Ppiase+Domain+Is+Marked+By+The+Bound+...'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIN OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: rotamase]] | [[Category: rotamase]] | ||
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Revision as of 11:00, 3 February 2008
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PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
OverviewOverview
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.
About this StructureAbout this Structure
1PIN is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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
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