1fin: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fin]] is a 4 chain structure with 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=1FIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FIN FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fin]] is a 4 chain structure with 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=1FIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FIN FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fin RCSB], [http://www.ebi.ac.uk/pdbsum/1fin PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fin RCSB], [http://www.ebi.ac.uk/pdbsum/1fin PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 33: | Line 33: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Jeffrey, P D | [[Category: Jeffrey, P D]] | ||
[[Category: Pavletich, N P | [[Category: Pavletich, N P]] | ||
[[Category: Russo, A A | [[Category: Russo, A A]] | ||
[[Category: Cdk]] | [[Category: Cdk]] | ||
[[Category: Cyclin]] | [[Category: Cyclin]] | ||
[[Category: Phosphorylation]] | [[Category: Phosphorylation]] |
Revision as of 03:43, 23 December 2014
CYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEXCYCLIN A-CYCLIN-DEPENDENT KINASE 2 COMPLEX
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex.,Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP Nature. 1995 Jul 27;376(6538):313-20. PMID:7630397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
|