1xox is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
NMR studies of the antiapoptotic protein survivin have been used to determine the homodimer interface of the protein in solution and to identify residues of the protein that interact with Smac/Diablo. In solution, survivin(1-120) forms a bow-tie-shaped dimer whose interface is composed of its N-terminal residues as well as residues connecting its BIR domain to the C-terminal alpha helix. The solution structure resolves the controversy regarding the two possible dimer interfaces for survivin observed in X-ray crystal structures. The structural basis for the interaction between survivin and Smac/Diablo was also investigated. When Smac/Diablo or N-terminal Smac/Diablo peptide analogues are added to a solution of survivin, specific residues near alpha4 and beta3 are perturbed. NMR experiments indicate that the peptides bind across the third beta-strand of survivin in a manner similar to the way Smac/Diablo peptides bind to the BIR3 domain of X-linked IAP (XIAP).
Solution structure of human survivin and its binding interface with Smac/Diablo.,Sun C, Nettesheim D, Liu Z, Olejniczak ET Biochemistry. 2005 Jan 11;44(1):11-7. PMID:15628841[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Sun C, Nettesheim D, Liu Z, Olejniczak ET. Solution structure of human survivin and its binding interface with Smac/Diablo. Biochemistry. 2005 Jan 11;44(1):11-7. PMID:15628841 doi:10.1021/bi0485171
