1jkl
From Proteopedia
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|PDB= 1jkl |SIZE=350|CAPTION= <scene name='initialview01'>1jkl</scene>, resolution 1.62Å | |PDB= 1jkl |SIZE=350|CAPTION= <scene name='initialview01'>1jkl</scene>, resolution 1.62Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | + | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jkl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jkl OCA], [http://www.ebi.ac.uk/pdbsum/1jkl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jkl RCSB]</span> | ||
}} | }} | ||
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[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
[[Category: Watterson, D M.]] | [[Category: Watterson, D M.]] | ||
| - | [[Category: ANP]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:02 2008'' |
Revision as of 18:35, 30 March 2008
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| , resolution 1.62Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.6A X-RAY STRUCTURE OF BINARY COMPLEX OF A CATALYTIC DOMAIN OF DEATH-ASSOCIATED PROTEIN KINASE WITH ATP ANALOGUE
Overview
We have determined X-ray crystal structures with up to 1.5 A resolution of the catalytic domain of death-associated protein kinase (DAPK), the first described member of a novel family of pro-apoptotic and tumor-suppressive serine/threonine kinases. The geometry of the active site was studied in the apo form, in a complex with nonhydrolyzable AMPPnP and in a ternary complex consisting of kinase, AMPPnP and either Mg2+ or Mn2+. The structures revealed a previously undescribed water-mediated stabilization of the interaction between the lysine that is conserved in protein kinases and the beta- and gamma-phosphates of ATP, as well as conformational changes at the active site upon ion binding. Comparison between these structures and nucleotide triphosphate complexes of several other kinases disclosed a number of unique features of the DAPK catalytic domain, among which is a highly ordered basic loop in the N-terminal domain that may participate in enzyme regulation.
About this Structure
1JKL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression., Tereshko V, Teplova M, Brunzelle J, Watterson DM, Egli M, Nat Struct Biol. 2001 Oct;8(10):899-907. PMID:11573098
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