1q59: Difference between revisions

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<StructureSection load='1q59' size='340' side='right'caption='[[1q59]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1q59' size='340' side='right'caption='[[1q59]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1q59]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebvg Ebvg]. 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://proteopedia.org/fgij/fg.htm?mol=1Q59 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1q59]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebvg Ebvg]. 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='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 EBVG])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BHRF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 EBVG])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1q59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q59 OCA], [http://pdbe.org/1q59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q59 RCSB], [http://www.ebi.ac.uk/pdbsum/1q59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q59 ProSAT]</span></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>
</table>
== Function ==
== Function ==
[[http://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.  
[[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.  
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 09:26, 2 March 2022

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

1q59 is a 1 chain structure with sequence from Ebvg. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:BHRF1 (EBVG)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Huang Q, Petros AM, Virgin HW, Fesik SW, Olejniczak ET. Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2. J Mol Biol. 2003 Oct 3;332(5):1123-30. PMID:14499614
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