We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2i53

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i53.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2i53.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i53| PDB=2i53 | SCENE= }}
{{STRUCTURE_2i53| PDB=2i53 | SCENE= }}
-
'''Crystal structure of Cyclin K'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17169370}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17169370 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17169370}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Positive transcription elongation factor]]
[[Category: Positive transcription elongation factor]]
[[Category: Transcription]]
[[Category: Transcription]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:04:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:43:34 2008''

Revision as of 02:43, 28 July 2008

Image:2i53.png

Template:STRUCTURE 2i53

Crystal structure of Cyclin K

Template:ABSTRACT PUBMED 17169370

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

Page seeded by OCA on Mon Jul 28 05:43:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i53"
Personal tools