1aow
From Proteopedia
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ANNEXIN IV
Overview
The structure of a trigonal crystal form of N-terminally truncated, [des-(1-9)] bovine annexin IV, an annexin variant that exhibits the, distinctive property of binding both phospholipids and carbohydrates in a, Ca2+-dependent manner, has been determined at 3 A (0.3 nm) resolution, -space group: R3; cell parameters: a=b=118.560 (8) A and c=82.233 (6) A-., The overall structure of annexin IV, crystallized in the absence of Ca2+, ions, is highly homologous to that of the other known members of the, annexin family. The trimeric assembly in the trigonal crystals of annexin, IV is quite similar to that found previously in non-isomorphous crystals, of human, chicken and rat annexin V and to the subunit arrangement in half, of the hexamer of hydra annexin XII. Moreover, it resembles that found in, two-dimensional crystals of human annexin V bound to phospholipid, monolayers. The propensity of several annexins to generate similar, trimeric arrays supports the hypothesis that trimeric complexes of such, annexins, including annexin IV, may represent the functional units that, interact with membranes.
About this Structure
1AOW is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of the trigonal crystal form of bovine annexin IV., Zanotti G, Malpeli G, Gliubich F, Folli C, Stoppini M, Olivi L, Savoia A, Berni R, Biochem J. 1998 Jan 1;329 ( Pt 1):101-6. PMID:9405281
Page seeded by OCA on Tue Nov 20 11:00:49 2007
