1q59: Difference between revisions
New page: left|200px<br /><applet load="1q59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q59" /> '''Solution Structure of the BHRF1 Protein From... |
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'''Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2'''<br /> | '''Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2'''<br /> | ||
==Overview== | ==Overview== | ||
The three-dimensional structure of BHRF1, the Bcl-2 homolog from | 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. | ||
==About this Structure== | ==About this Structure== | ||
1Q59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http:// | 1Q59 is a [http://en.wikipedia.org/wiki/Single_protein 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fesik, S | [[Category: Fesik, S W.]] | ||
[[Category: Huang, Q.]] | [[Category: Huang, Q.]] | ||
[[Category: Olejniczak, E | [[Category: Olejniczak, E T.]] | ||
[[Category: Petros, A | [[Category: Petros, A M.]] | ||
[[Category: Virgin, H | [[Category: Virgin, H W.]] | ||
[[Category: bcl-2]] | [[Category: bcl-2]] | ||
[[Category: bhrf1]] | [[Category: bhrf1]] | ||
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[[Category: structure determination]] | [[Category: structure determination]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:02 2008'' | ||
Revision as of 15:36, 21 February 2008
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Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
OverviewOverview
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.
About this StructureAbout this Structure
1Q59 is a Single protein structure of sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
ReferenceReference
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
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