The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes

Huber, R.; Römisch, J.; Paques, E.P.

EMBO Journal 9(12): 3867-3874

1990


ISSN/ISBN: 0261-4189
PMID: 2147412
Document Number: 366306
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.

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