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[[Image:1vin.gif|left|200px]]<br /><applet load="1vin" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vin, resolution 2.0&Aring;" />
'''BOVINE CYCLIN A3'''<br />


==Overview==
==BOVINE CYCLIN A3==
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.
<StructureSection load='1vin' size='340' side='right'caption='[[1vin]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vin]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VIN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vin OCA], [https://pdbe.org/1vin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vin RCSB], [https://www.ebi.ac.uk/pdbsum/1vin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vin ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCNA2_BOVIN CCNA2_BOVIN] Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vi/1vin_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vin ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1VIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIN OCA].
*[[Cyclin 3D structures|Cyclin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591034 8591034]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brown, N R.]]
[[Category: Brown NR]]
[[Category: Endicott, J A.E.]]
[[Category: Endicott JAE]]
[[Category: Noble, M E.M.]]
[[Category: Noble MEM]]
[[Category: binding protein]]
[[Category: cell cycle]]
[[Category: cyclin]]
[[Category: kinase-regulatory-subunit]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:44 2008''

Latest revision as of 11:46, 14 February 2024

BOVINE CYCLIN A3BOVINE CYCLIN A3

Structural highlights

1vin is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCNA2_BOVIN Essential for the control of the cell cycle at the G1/S (start) and the G2/M (mitosis) transitions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1vin, resolution 2.00Å

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