1vin
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1vin.gif|left|200px]] | [[Image:1vin.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1vin", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1vin| PDB=1vin | SCENE= }} | |
| - | + | ||
| - | | | + | |
| - | }} | + | |
'''BOVINE CYCLIN A3''' | '''BOVINE CYCLIN A3''' | ||
| Line 28: | Line 25: | ||
[[Category: Endicott, J A.E.]] | [[Category: Endicott, J A.E.]] | ||
[[Category: Noble, M E.M.]] | [[Category: Noble, M E.M.]] | ||
| - | [[Category: | + | [[Category: Binding protein]] |
| - | [[Category: | + | [[Category: Cell cycle]] |
| - | [[Category: | + | [[Category: Cyclin]] |
| - | [[Category: | + | [[Category: Kinase-regulatory-subunit]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:34:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:34, 3 May 2008
BOVINE CYCLIN A3
Overview
BACKGROUND: Eukaryotic cell cycle progression is regulated by cyclin dependent protein kinases (CDKs) whose activity is regulated by association with cyclins and by reversible phosphorylation. Cyclins also determine the subcellular location and substrate specificity of CDKs. Cyclins exhibit diverse sequences but all share homology over a region of approximately 100 amino acids, termed the cyclin box. From the determination of the structure of cyclin A, together with results from biochemical and genetic analyses, we can identify which parts of the cyclin molecular may contribute to cyclin A structure and function. RESULTS: We have solved the crystal structure, at 2.0 A resolution, of an active recombinant fragment of bovine cyclin A, cyclin A-3, corresponding to residues 171-432 of human cyclin A. The cyclin box has an alpha-helical fold comprising five alpha helices. This fold is repeated in the C-terminal region, although this region shares negligible sequence similarity with the cyclin box. CONCLUSIONS: Analysis of residues that are conserved throughout the A, B, and E cyclins identifies two exposed clusters of residues, one of which has recently been shown to be involved in the association with human CDK2. The second cluster may identify another site of cyclin A-protein interaction. Comparison of the structure of the unbound cyclin with the structure of cyclin A complexed with CDK2 reveals that cyclin A does not undergo any significant conformational changes on complex formation. Threading analysis shows that the cyclin-box fold is consistent with the sequences of the transcription factor TFIIB and other functionally related proteins. The structural results indicate a role for the cyclin-box fold both as a template for the cyclin family and as a generalised adaptor molecule in the regulation of transcription.
About this Structure
1VIN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The crystal structure of cyclin A., Brown NR, Noble ME, Endicott JA, Garman EF, Wakatsuki S, Mitchell E, Rasmussen B, Hunt T, Johnson LN, Structure. 1995 Nov 15;3(11):1235-47. PMID:8591034 Page seeded by OCA on Sat May 3 12:34:27 2008
