1fin: Difference between revisions

Line 4:

==Overview==

The crystal structure of the human cyclinA-cyclin-dependent kinase2, (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds, to one side of CDK2's catalytic cleft, inducing large conformational, changes in its PSTAIRE helix and T-loop. These changes activate the kinase, by realigning active site residues and relieving the steric blockade at, the entrance of the catalytic cleft.

The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.

==About this Structure==

Line 13:

[[Category: Homo sapiens]]

[[Category: Protein complex]]

[[Category: Jeffrey, P.D.]]

[[Category: Jeffrey, P D.]]

[[Category: Pavletich, N.P.]]

[[Category: Pavletich, N P.]]

[[Category: Russo, A.A.]]

[[Category: Russo, A A.]]

[[Category: ATP]]

[[Category: cdk]]

Line 22:

[[Category: phosphorylation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:47:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:02 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-The crystal structure of the human cyclinA-cyclin-dependent kinase2, (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds, to one side of CDK2's catalytic cleft, inducing large conformational, changes in its PSTAIRE helix and T-loop. These changes activate the kinase, by realigning active site residues and relieving the steric blockade at, the entrance of the catalytic cleft.
+The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft, inducing large conformational changes in its PSTAIRE helix and T-loop. These changes activate the kinase by realigning active site residues and relieving the steric blockade at the entrance of the catalytic cleft.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Protein complex]]
-[[Category: Jeffrey, P.D.]]
+[[Category: Jeffrey, P D.]]
-[[Category: Pavletich, N.P.]]
+[[Category: Pavletich, N P.]]
-[[Category: Russo, A.A.]]
+[[Category: Russo, A A.]]
 [[Category: ATP]]
 [[Category: cdk]]
@@ Line 22: / Line 22: @@
 [[Category: phosphorylation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:47:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:02 2008''