THE CRYSTAL AND MOLECULAR-STRUCTURE OF HUMAN ANNEXIN-V, AN ANTICOAGULANT PROTEIN THAT BINDS TO CALCIUM AND MEMBRANES
THE CRYSTAL AND MOLECULAR-STRUCTURE OF HUMAN ANNEXIN-V, AN ANTICOAGULANT PROTEIN THAT BINDS TO CALCIUM AND MEMBRANES
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DOI：
10.1002/j.1460-2075.1990.tb07605.x
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发表时间：
1990-12-01
期刊：
影响因子：
11.4
通讯作者：
PAQUES, EP
中科院分区：
文献类型：
--
作者：
HUBER, R;ROMISCH, J;PAQUES, EP
人膜联蛋白V（PP4），钙家族的膜，膜结合蛋白，已经在钙存在下结晶，并通过在3埃的多个同晶置换进行晶体学分析。并在2.5.ANG下进行初步细化。分辨率该分子的尺寸为64 × 104。40倍30.ANG.3，并折叠成四个结构相似的结构域。每个域由五个α-螺旋缠绕成右旋超螺旋，产生apprx的球状结构。18.角直径.结构域具有疏水核心，其氨基酸序列在结构域之间和蛋白质的膜联蛋白家族内是保守的。通过结构域II和III以及I和IV的紧密（疏水）成对包装将四个结构域折叠成几乎平面的阵列，以分别产生模块（II-III）和（I-IV）。该组件是对称的，具有三个平行的近似二元组，分别涉及II到III，I到IV和模块（II-III）到（I-IV）。后一个二联体标记了一个通道，该通道穿过被带电荷的氨基酸残基包覆的分子中心。该蛋白具有通道形成膜蛋白的结构特征和可溶性蛋白的极性表面特征。它是不同于可溶性蛋白和膜蛋白的第三类两亲蛋白的成员。
Human annexin V (PP4), a membrane of the family of calcium, membrane binding proteins, has been crystallized in the presence of calcium and analysed by crystallography by multiple isomorphic replacement at 3 .ANG. and preliminarily refined at 2.5 .ANG. resolution. The molecule has dimensions of 64 .times. 40 .times. 30 .ANG.3 and is folded into four domains of similar structure. Each domains consists of five .alpha.-helices wound into a right-handed superhelix yielding a globular structure of .apprx. 18 .ANG. diameter. The domains have hydrophobic cores whose amino acid sequences are conserved between the domains and within the annexin family of proteins. The four domains are folded into an almost planar array by tight (hydrophobic) pair-wise packing of domains II and III and I and IV to generate modules (II-III) and (I-IV), respectively. The assembly is symmetric with three parallel approximate diads relating II to III, I to IV and the module (II-III) to (I-IV), respectively. The latter diad marks a channel through the centre of the molecule coated with charged amino acid residues. The protein has structural features of channel forming membrane proteins and a polar surface characteristic of soluble proteins. It is a member of the third class of amphipathic proteins different from soluble and membrane proteins.