Hinds M G, Norton R S, Vaux D L, Day C L
Biomolecular Research Institute, Parkville, Australia.
Nat Struct Biol. 1999 Jul;6(7):648-51. doi: 10.1038/10701.
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.
凋亡抑制蛋白（IAP）家族的成员能够在病毒感染后、发育过程中或体外细胞系中抑制细胞死亡。所有IAP蛋白都带有一个或多个杆状病毒IAP重复序列（BIR）。在此，我们描述了来自哺乳动物IAP同源物B（MIHB/c-IAP-1）的第三个BIR结构域的溶液结构。BIR结构域具有一种新颖的折叠方式，由一个组氨酸和三个半胱氨酸残基以四面体方式配位的锌来稳定。该结构由一系列短的α螺旋和转角组成，锌被包裹在一个由所有BIR中高度保守的残基形成的异常疏水的环境中。
