1qbh
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(New page: 200px<br /> <applet load="1qbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qbh" /> '''SOLUTION STRUCTURE OF A BACULOVIRAL INHIBIT...)
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Revision as of 16:45, 12 November 2007
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SOLUTION STRUCTURE OF A BACULOVIRAL INHIBITOR OF APOPTOSIS (IAP) REPEAT
Overview
Members of the inhibitor of apoptosis (IAP) family of proteins are able to, inhibit cell death following viral infection, during development or in, cell lines in vitro. All IAP proteins bear one or more baculoviral IAP, repeats (BIRs). Here we describe the solution structure of the third BIR, domain from the mammalian IAP homolog B (MIHB/c-IAP-1). The BIR domain has, a novel fold that is stabilized by zinc tetrahedrally coordinated by one, histidine and three cysteine residues. The structure consists of a series, of short alpha-helices and turns with the zinc packed in an unusually, hydrophobic environment created by residues that are highly conserved, among all BIRs.
About this Structure
1QBH is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat., Hinds MG, Norton RS, Vaux DL, Day CL, Nat Struct Biol. 1999 Jul;6(7):648-51. PMID:10404221
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