1pin: Difference between revisions

Revision as of 13:55, 30 April 2008

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. 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 Page seeded by OCA on Wed Apr 30 13:55:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 [[Image:1pin.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1pin |SIZE=350|CAPTION= <scene name='initialview01'>1pin</scene>, resolution 1.35&Aring;
+The line below this paragraph, containing "STRUCTURE_1pin", creates the "Structure Box" on the page.
-|SITE= <scene name='pdbsite=ACT:The+Active+Site+Of+Ppiase+Domain+Is+Marked+By+The+Bound+...'>ACT</scene>
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=1PG:2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL'>1PG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE= PIN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+-->
-|DOMAIN=
+{{STRUCTURE_1pin|  PDB=1pin  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pin OCA], [http://www.ebi.ac.uk/pdbsum/1pin PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pin RCSB]</span>
-}}
 '''PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS'''
@@ Line 29: / Line 26: @@
 [[Category: Noel, J P.]]
 [[Category: Ranganathan, R.]]
-[[Category: complex (isomerase/dipeptide)]]
+[[Category: Peptidyl-prolyl cis-trans isomerase]]
-[[Category: peptidyl-prolyl cis-trans isomerase]]
+[[Category: Rotamase]]
-[[Category: rotamase]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:55:24 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:09 2008''