Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor.
Article Details
- CitationCopy to clipboard
Kaneko N, Ago H, Matsuda R, Inagaki E, Miyano M
Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor.
J Mol Biol. 1997 Nov 21;274(1):16-20.
- PubMed ID
- 9398511 [ View in PubMed]
- Abstract
The crystal structure of recombinant human annexin V complexed with K-201, an inhibitor of the calcium ion channel activity of annexin V, was solved at 3.0 A by molecular replacement including the apo and high-calcium forms. K-201 was bound at the hinge region cavity formed by the N-terminal strand and domains II, III and IV, at the side opposite the calcium and membrane-binding surface, in an L-shaped conformation. Based on the complex and other annexin structures, K-201 is proposed to restrain the hinge movement of annexin V in an allosteric manner, resulting in the inhibition of calcium movement across the annexin V molecule.