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]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1q59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 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 [https://proteopedia.org/fgij/fg.htm?mol=1Q59 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1q59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q59 OCA], [https://pdbe.org/1q59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q59 RCSB], [https://www.ebi.ac.uk/pdbsum/1q59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q59 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EAR_EBVB9 EAR_EBVB9] Prevents premature death of the host cell during virus production, which would otherwise reduce the amount of progeny virus. Acts as a host B-cell leukemia/lymphoma 2 (Bcl-2) homolog, and interacts with pro-apoptotic proteins to prevent mitochondria permeabilization, release of cytochrome c and subsequent apoptosis of the host cell. | |||
<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> | |||
== | <div class="pdbe-citations 1q59" style="background-color:#fffaf0;"></div> | ||
[[ | == References == | ||
[[Category: | <references/> | ||
[[Category: Fesik | __TOC__ | ||
[[Category: Huang | </StructureSection> | ||
[[Category: Olejniczak | [[Category: Human gammaherpesvirus 4]] | ||
[[Category: Petros | [[Category: Large Structures]] | ||
[[Category: Virgin | [[Category: Fesik SW]] | ||
[[Category: Huang Q]] | |||
[[Category: Olejniczak ET]] | |||
[[Category: Petros AM]] | |||
[[Category: Virgin HW]] | |||
Latest revision as of 12:18, 6 December 2023
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
FunctionEAR_EBVB9 Prevents premature death of the host cell during virus production, which would otherwise reduce the amount of progeny virus. Acts as a host B-cell leukemia/lymphoma 2 (Bcl-2) homolog, and interacts with pro-apoptotic proteins to prevent mitochondria permeabilization, release of cytochrome c and subsequent apoptosis of the host cell. 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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