2h9v: Difference between revisions

Line 1:

[[Image:2h9v.~~gif~~|left|200px]]

[[Image:2h9v.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632~~'''~~

===Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632===

~~==Overview==~~

<!--

Rho-kinase is a main player in the regulation of cytoskeletal events and a promising drug target in the treatment of both vascular and neurological disorders. Here we report the crystal structure of the Rho-~~kinase catalytic domain in complex with the specific inhibitor Y~~-~~27632. Comparison with~~ the ~~structure of PKA bound~~ to ~~this inhibitor revealed a potential induced-fit binding mode that can be accommodated by~~ the ~~phosphate binding loop~~. ~~This binding mode resembles to that observed in~~ the ~~Rho-kinase-fasudil complex~~. ~~A structural database search indicated that a pocket underneath the phosphate~~-~~binding loop is present that favors binding to a small aromatic ring. Introduction of such a ring group might spawn a new modification scheme of pre~~-~~existing protein kinase inhibitors for improved binding capability.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16891330}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16891330 is the PubMed ID number.

-->

==About this Structure==

Line 31:

Line 35:

[[Category: Yamaguchi, H.]]

[[Category: Protein kinase-inhibitor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 06~~:02:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:08:37 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:2h9v.gif|left|200px]]
+{{Seed}}
+[[Image:2h9v.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2h9v|  PDB=2h9v  |  SCENE=  }}
-'''Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632'''
+===Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632===
-==Overview==
+<!--
-Rho-kinase is a main player in the regulation of cytoskeletal events and a promising drug target in the treatment of both vascular and neurological disorders. Here we report the crystal structure of the Rho-kinase catalytic domain in complex with the specific inhibitor Y-27632. Comparison with the structure of PKA bound to this inhibitor revealed a potential induced-fit binding mode that can be accommodated by the phosphate binding loop. This binding mode resembles to that observed in the Rho-kinase-fasudil complex. A structural database search indicated that a pocket underneath the phosphate-binding loop is present that favors binding to a small aromatic ring. Introduction of such a ring group might spawn a new modification scheme of pre-existing protein kinase inhibitors for improved binding capability.
+The line below this paragraph, {{ABSTRACT_PUBMED_16891330}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16891330 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16891330}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Yamaguchi, H.]]
 [[Category: Protein kinase-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:02:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:08:37 2008''