Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat
- Author(s)
- Hinds, MG; Norton, RS; Vaux, DL; Day, CL;
- Details
- Publication Year 1999-07,Volume 6,Issue #7,Page 648-651
- Journal Title
- NATURE STRUCTURAL BIOLOGY
- Publication Type
- Journal Article
- Abstract
- 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 pip domain from the mammalian IAP homolog B (MIHB/c-IAP-1). The pip 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 cc-helices and turns with the zinc packed in an unusually hydrophobic environment created by residues that are highly conserved among all BIRs.
- Publisher
- NATURE AMERICA INC
- Keywords
- PROGRAMMED CELL-DEATH; NMR STRUCTURE; PROTEIN STRUCTURES; MAMMALIAN-CELLS; GENE; ZINC; MUTAGENESIS; CASPASES; DYNAMICS; HOMOLOGS
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- Refer to copyright notice on published article.
Creation Date: 1999-07-01 12:00:00