1q59: Difference between revisions
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[[ | ==Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2== | ||
<StructureSection load='1q59' size='340' side='right' caption='[[1q59]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1q59]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q59 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BHRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 Human herpesvirus 4])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q59 RCSB], [http://www.ebi.ac.uk/pdbsum/1q59 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The three-dimensional structure of BHRF1, the Bcl-2 homolog from Epstein-Barr virus (EBV), has been determined by NMR spectroscopy. Although the overall structure is similar to other Bcl-2 family members, there are important structural differences. Unlike some of the other Bcl-2 family members, BHRF1 does not contain the prominent hydrophobic groove that mediates binding to pro-apoptotic family members. In addition, in contrast to the anti-apoptotic Bcl-2 proteins, BHRF1 does not bind tightly to peptides derived from the pro-apoptotic proteins Bak, Bax, Bik, and Bad. The lack of an exposed, pre-formed binding groove in BHRF1 and the lack of significant binding to peptides derived from pro-apoptotic family members that bind to other anti-apoptotic family members, suggest that the mechanism of the BHRF1 anti-apoptotic activity does not parallel that of cellular Bcl-x(L) or Bcl-2. | |||
Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2.,Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET J Mol Biol. 2003 Oct 3;332(5):1123-30. PMID:14499614<ref>PMID:14499614</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Fesik, S W.]] | [[Category: Fesik, S W.]] | ||
Revision as of 11:30, 8 October 2014
Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
Structural highlights
Publication Abstract from PubMedThe three-dimensional structure of BHRF1, the Bcl-2 homolog from Epstein-Barr virus (EBV), has been determined by NMR spectroscopy. Although the overall structure is similar to other Bcl-2 family members, there are important structural differences. Unlike some of the other Bcl-2 family members, BHRF1 does not contain the prominent hydrophobic groove that mediates binding to pro-apoptotic family members. In addition, in contrast to the anti-apoptotic Bcl-2 proteins, BHRF1 does not bind tightly to peptides derived from the pro-apoptotic proteins Bak, Bax, Bik, and Bad. The lack of an exposed, pre-formed binding groove in BHRF1 and the lack of significant binding to peptides derived from pro-apoptotic family members that bind to other anti-apoptotic family members, suggest that the mechanism of the BHRF1 anti-apoptotic activity does not parallel that of cellular Bcl-x(L) or Bcl-2. Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2.,Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET J Mol Biol. 2003 Oct 3;332(5):1123-30. PMID:14499614[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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