1bu2: Difference between revisions

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New page: left|200px<br /><applet load="1bu2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bu2, resolution 3.00Å" /> '''X-RAY STRUCTURE OF A...
 
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[[Image:1bu2.jpg|left|200px]]<br /><applet load="1bu2" size="450" color="white" frame="true" align="right" spinBox="true"
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'''X-RAY STRUCTURE OF A VIRAL CYCLIN FROM HERPESVIRUS SAIMIRI'''<br />


==Overview==
==X-RAY STRUCTURE OF A VIRAL CYCLIN FROM HERPESVIRUS SAIMIRI==
BACKGROUND: Cyclin-dependent kinases (CDKs) have a central role in, cell-cycle control and are activated by complex formation with positive, regulatory proteins called cyclins and by phosphorylation. The, overexpression and mutation of cyclins and CDKs has been associated with, tumorigenesis and oncogenesis. A virus-encoded cyclin (v-cyclin) from, herpesvirus saimiri has been shown to exhibit highest sequence homology to, type D cyclins and specifically activates CDK6 of host cells to a very, high degree. RESULTS: We have determined the first X-ray structure of a, v-cyclin to 3.0 A resolution. The structure of the core domains is very, similar to those of cyclin A and cyclin H from human cells. To understand, the structural basis for the v-cyclin specificity for CDK6 and the, insensitivity of the complex to inhibitors of the p21 and INK4 families, a, v-cyclin-CDK2 model was built on the basis of the known structures of, human cyclin A in complex with CDK2 and the CDK inhibitor p27(Kip1)., CONCLUSIONS: Although many critical interactions between cyclin A and CDK2, would be conserved in a v-cyclin-CDK2 complex, some appear sterically or, electrostatically unfavorable due to shifts in the backbone conformation, or sidechain differences and may contribute to v-cyclin selectivity for, CDK6. The insensitivity of v-cyclin-CDK6 complexes to inhibitors of the, p21 family is probably due to structural changes in v-cyclin that lead to, a flatter surface area offering fewer potential contacts with the protein, inhibitor. In addition, sequence changes in v-cyclin eliminate, hydrogen-bonding partners for atoms of the p27(Kip1) inhibitor. This, structure provides the first model for interactions between v-cyclins and, host cell-cycle proteins; these interactions may be important for virus, survival as well as oncogenic transformation of host cells.
<StructureSection load='1bu2' size='340' side='right'caption='[[1bu2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bu2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Herpesvirus_saimiri_(strain_11) Herpesvirus saimiri (strain 11)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BU2 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]] 3&#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=1bu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bu2 OCA], [https://pdbe.org/1bu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1bu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bu2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CGH2_SHV21 CGH2_SHV21] May be highly relevant to the process of cellular transformation and rapid T-cell proliferation effected by HVS during latent infections of T-cells in susceptible hosts.
== 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/bu/1bu2_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=1bu2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BU2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saimiriine_herpesvirus_3 Saimiriine herpesvirus 3]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BU2 OCA].
*[[Cyclin 3D structures|Cyclin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of a viral cyclin, a positive regulator of cyclin-dependent kinase 6., Schulze-Gahmen U, Jung JU, Kim SH, Structure. 1999 Mar 15;7(3):245-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368294 10368294]
[[Category: Large Structures]]
[[Category: Saimiriine herpesvirus 3]]
[[Category: Jung JU]]
[[Category: Single protein]]
[[Category: Kim S-H]]
[[Category: Jung, J.U.]]
[[Category: Schulze-Gahmen U]]
[[Category: Kim, S.H.]]
[[Category: Schulze-Gahmen, U.]]
[[Category: cell cycle regulation]]
[[Category: herpesvirus saimiri]]
[[Category: viral cyclin]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:55:17 2007''

Latest revision as of 09:39, 7 February 2024

X-RAY STRUCTURE OF A VIRAL CYCLIN FROM HERPESVIRUS SAIMIRIX-RAY STRUCTURE OF A VIRAL CYCLIN FROM HERPESVIRUS SAIMIRI

Structural highlights

1bu2 is a 1 chain structure with sequence from Herpesvirus saimiri (strain 11). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CGH2_SHV21 May be highly relevant to the process of cellular transformation and rapid T-cell proliferation effected by HVS during latent infections of T-cells in susceptible hosts.

Evolutionary Conservation

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

See Also

1bu2, resolution 3.00Å

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