1hak: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: placenta anticoagulant protein-i]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:17 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 25: / Line 25: @@
 [[Category: placenta anticoagulant protein-i]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:17 2008''