2i53
From Proteopedia
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|PDB= 2i53 |SIZE=350|CAPTION= <scene name='initialview01'>2i53</scene>, resolution 1.50Å | |PDB= 2i53 |SIZE=350|CAPTION= <scene name='initialview01'>2i53</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= CCNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CCNK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jkw|1JKW]], [[1kxu|1KXU]], [[1vin|1VIN]], [[1bu2|1BU2]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i53 OCA], [http://www.ebi.ac.uk/pdbsum/2i53 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i53 RCSB]</span> | ||
}} | }} | ||
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[[Category: Brown, R S.]] | [[Category: Brown, R S.]] | ||
[[Category: Ladias, J A.A.]] | [[Category: Ladias, J A.A.]] | ||
| - | [[Category: ACT]] | ||
[[Category: cdk9]] | [[Category: cdk9]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:53 2008'' |
Revision as of 00:40, 31 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | CCNK (Homo sapiens) | ||||||
| Related: | 1JKW, 1KXU, 1VIN, 1BU2
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Cyclin K
Overview
Cyclin K and the closely related cyclins T1, T2a, and T2b interact with cyclin-dependent kinase 9 (CDK9) forming multiple nuclear complexes, referred to collectively as positive transcription elongation factor b (P-TEFb). Through phosphorylation of the C-terminal domain of the RNA polymerase II largest subunit, distinct P-TEFb species regulate the transcriptional elongation of specific genes that play central roles in human physiology and disease development, including cardiac hypertrophy and human immunodeficiency virus-1 pathogenesis. We have determined the crystal structure of human cyclin K (residues 11-267) at 1.5 A resolution, which represents the first atomic structure of a P-TEFb subunit. The cyclin K fold comprises two typical cyclin boxes with two short helices preceding the N-terminal box. A prominent feature of cyclin K is an additional helix (H4a) in the first cyclin box that obstructs the binding pocket for the cell-cycle inhibitor p27(Kip1). Modeling of CDK9 bound to cyclin K provides insights into the structural determinants underlying the formation and regulation of this complex. A homology model of human cyclin T1 generated using the cyclin K structure as a template reveals that the two proteins have similar structures, as expected from their high level of sequence identity. Nevertheless, their CDK9-interacting surfaces display significant structural differences, which could potentially be exploited for the design of cyclin-targeted inhibitors of the CDK9-cyclin K and CDK9-cyclin T1 complexes.
About this Structure
2I53 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human cyclin K, a positive regulator of cyclin-dependent kinase 9., Baek K, Brown RS, Birrane G, Ladias JA, J Mol Biol. 2007 Feb 16;366(2):563-73. Epub 2006 Nov 18. PMID:17169370
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