2csn
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2csn.jpg|left|200px]] | [[Image:2csn.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2csn", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2csn| PDB=2csn | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7''' | '''BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7''' | ||
| Line 27: | Line 24: | ||
[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
[[Category: Xu, R M.]] | [[Category: Xu, R M.]] | ||
| - | [[Category: | + | [[Category: Casein kinase-1]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:57:52 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:57, 3 May 2008
BINARY COMPLEX OF CASEIN KINASE-1 WITH CKI7
Overview
A large family of isoquinoline sulfonamide compounds inhibits protein kinases by competing with adenosine triphosphates(ATP), yet interferes little with the activity of other ATP-using enzymes such as ATPases and adenylate cyclases. One such compound, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide (CK17), is selective for casein kinase-1 isolated from a variety of sources. Here we report the crystal structure of the catalytic domain of Schizosaccharomyces pombe casein kinase-1 complexed with CK17, refined to a crystallographic R-factor of 17.8% at 2.5 angstrom resolution. The structure provides new insights into the mechanism of the ATP-competing inhibition and the origin of their selectivity toward different protein kinases. Selectivity for protein kinases versus other enzymes is achieved by hydrophobic contacts and the hydrogen bond with isoquinoline ring. We propose that the hydrogen bond involving the ring nitrogen-2 atom of the isoquinoline must be preserved, but that the ring can flip depending on the chemical substituents at ring positions 5 and 8. Selectivity for individual members of the protein kinase family is achieved primarily by interactions with these substituents.
About this Structure
2CSN is a Single protein structure of sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors., Xu RM, Carmel G, Kuret J, Cheng X, Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6308-13. PMID:8692811 Page seeded by OCA on Sat May 3 22:57:52 2008
