1q59

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[[Image:1q59.gif|left|200px]]
 
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{{Structure
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==Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2==
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|PDB= 1q59 |SIZE=350|CAPTION= <scene name='initialview01'>1q59</scene>
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<StructureSection load='1q59' size='340' side='right'caption='[[1q59]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= BHRF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 Human herpesvirus 4])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1q59 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q59 RCSB]</span>
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[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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}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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'''Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2'''
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==Overview==
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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.
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.
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==About this Structure==
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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>
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1Q59 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q59 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14499614 14499614]
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[[Category: Human herpesvirus 4]]
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[[Category: Single protein]]
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[[Category: Fesik, S W.]]
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[[Category: Huang, Q.]]
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[[Category: Olejniczak, E T.]]
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[[Category: Petros, A M.]]
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[[Category: Virgin, H W.]]
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[[Category: bcl-2]]
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[[Category: bhrf1]]
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[[Category: epstein-barr virus]]
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[[Category: nmr spectroscopy]]
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[[Category: structure determination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:08:58 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1q59" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Human gammaherpesvirus 4]]
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[[Category: Large Structures]]
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[[Category: Fesik SW]]
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[[Category: Huang Q]]
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[[Category: Olejniczak ET]]
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[[Category: Petros AM]]
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[[Category: Virgin HW]]

Current revision

Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2

PDB ID 1q59

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