1HAK

CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLACENTAL ANNEXIN V COMPLEXED WITH K-201 AS A CALCIUM CHANNEL ACTIVITY INHIBITOR

Summary for 1HAK

• Entry DOI: 10.2210/pdb1hak/pdb
• Descriptor: ANNEXIN V, 4-[3-{1-(4-BENZYL)PIPERODINYL}PROPIONYL]-7-METHOXY-2,3,4,5-TERTRAHYDRO-1,4-BENZOTHIAZEPINE (3 entities in total)
• Functional Keywords: annexin v, lipocortin v, endonexin ii, placenta anticoagulant protein-i, 35kda calelectrin, inhibitor of blood coagulation, calcium/phospholipid-binding, calcium-phospholipid-binding complex
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 72810.61

Authors

Ago, H.,Inagaki, E.,Miyano, M. (deposition date: 1997-12-10, release date: 1999-02-16, Last modification date: 2024-05-22)

Primary citation

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., 274:16-20, 1997

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.

PubMed: 9398511
DOI: 10.1006/jmbi.1997.1375

Experimental method

X-RAY DIFFRACTION (3 Å)