| Literature DB >> 1825119 |
G Mosser1, C Ravanat, J M Freyssinet, A Brisson.
Abstract
Two-dimensional crystals of annexin-V bound to lipid layers containing dioleoylphosphatidylserine have been obtained in the presence of Ca2+. The crystals diffract to 20 A resolution and have the symmetry of the plane group p3 (unit cell dimensions: a = b = 94 A, gamma = 120 degrees). Electron image analysis revealed that the crystals are composed of trimers of annexin-V forming triskelion-like motifs. Each annexin-V molecule has a characteristic elongated shape, about 65 A by 20 A, when observed perpendicularly to the crystal plane. It is composed of two staggered domains of similar size, about 40 A by 20 A. Both domains are made of two sub-domains. The present data suggest that the four resolved sub-domains represent the folding units corresponding to the four 70 amino acid repeating segments characteristic of all annexins.Entities:
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Year: 1991 PMID： 1825119 DOI： 10.1016/0022-2836(91)90538-h
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469