|
|
| Line 1: |
Line 1: |
| [[Image:2cn8.jpg|left|200px]] | | {{Seed}} |
| | [[Image:2cn8.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_2cn8| PDB=2cn8 | SCENE= }} | | {{STRUCTURE_2cn8| PDB=2cn8 | SCENE= }} |
|
| |
|
| '''CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH DEBROMOHYMENIALDISINE'''
| | ===CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH DEBROMOHYMENIALDISINE=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| The protein kinase Chk2 (checkpoint kinase 2) is a major effector of the replication checkpoint. Chk2 activation is initiated by phosphorylation of Thr68, in the serine-glutamine/threonine-glutamine cluster domain (SCD), by ATM. The phosphorylated SCD-segment binds to the FHA domain of a second Chk2 molecule, promoting dimerisation of the protein and triggering phosphorylation of the activation segment/T-loop in the kinase domain. We have now determined the structure of the kinase domain of human Chk2 in complexes with ADP and a small-molecule inhibitor debromohymenialdisine. The structure reveals a remarkable dimeric arrangement in which T-loops are exchanged between protomers, to form an active kinase conformation in trans. Biochemical data suggest that this dimer is the biologically active state promoted by ATM-phosphorylation, and also suggests a mechanism for dimerisation-driven activation of Chk2 by trans-phosphorylation. | | The line below this paragraph, {{ABSTRACT_PUBMED_16794575}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16794575 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_16794575}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 42: |
Line 46: |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| [[Category: Tumour suppressor]] | | [[Category: Tumour suppressor]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:34:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:57:09 2008'' |