1Q59
Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2
Summary for 1Q59
| Entry DOI | 10.2210/pdb1q59/pdb |
| Descriptor | Early antigen protein R (1 entity in total) |
| Functional Keywords | bhrf1, bcl-2, epstein-barr virus, nmr spectroscopy, structure determination, viral protein |
| Biological source | Human herpesvirus 4 (Epstein-Barr virus) |
| Cellular location | Host membrane; Single-pass membrane protein (Potential): P03182 |
| Total number of polymer chains | 1 |
| Total formula weight | 19848.25 |
| Authors | Huang, Q.,Petros, A.M.,Virgin, H.W.,Fesik, S.W.,Olejniczak, E.T. (deposition date: 2003-08-06, release date: 2003-09-23, Last modification date: 2024-05-22) |
| Primary citation | Huang, Q.,Petros, A.M.,Virgin, H.W.,Fesik, S.W.,Olejniczak, E.T. Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2 J.Mol.Biol., 332:1123-1130, 2003 Cited by PubMed Abstract: 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. PubMed: 14499614DOI: 10.1016/j.jmb.2003.08.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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