1K3K

Solution Structure of a Bcl-2 Homolog from Kaposi's Sarcoma Virus


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: AVERAGE, MINIMIZED 

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This is version 1.3 of the entry. See complete history


Literature

Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus.

Huang, Q.Petros, A.M.Virgin, H.W.Fesik, S.W.Olejniczak, E.T.

(2002) Proc Natl Acad Sci U S A 99: 3428-3433

  • DOI: https://doi.org/10.1073/pnas.062525799
  • Primary Citation of Related Structures:  
    1K3K

  • PubMed Abstract: 

    Kaposi sarcoma-associated herpes virus (KSHV) contains a gene that has functional and sequence homology to the apoptotic Bcl-2 family of proteins [Sarid, R., Sato, T., Bohenzky, R. A., Russo, J. J. & Chang, Y. (1997) Nat. Med. 3, 293-298]. The viral Bcl-2 protein promotes survival of infected cells and may contribute to the development of Kaposi sarcoma tumors [Boshoff, C. & Chang, Y. (2001) Annu. Rev. Med. 52, 453-470]. Here we describe the solution structure of the viral Bcl-2 homolog from KSHV. Comparison of the KSHV Bcl-2 structure to that of Bcl-2 and Bcl-x(L) shows that although the overall fold is the same, there are key differences in the lengths of the helices and loops. Binding studies on peptides derived from the Bcl-2 homology region 3 of proapoptotic family members indicate that the specificity of the viral protein is very different from what was previously observed for Bcl-x(L) and Bcl-2, suggesting that the viral protein has evolved to have a different mechanism of action than the host proteins.


  • Organizational Affiliation

    Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
functional anti-apoptotic factor vBCL-2 homolog158Human gammaherpesvirus 8Mutation(s): 2 
UniProt
Find proteins for Q76RI8 (Human herpesvirus 8)
Explore Q76RI8 
Go to UniProtKB:  Q76RI8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ76RI8
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: AVERAGE, MINIMIZED 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-04-10
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Database references, Derived calculations