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| {{STRUCTURE_2cko| PDB=2cko | SCENE= }} | | {{STRUCTURE_2cko| PDB=2cko | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA 2'''
| | ===CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA 2=== |
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| ==Overview==
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| Choline kinase, responsible for the phosphorylation of choline to phosphocholine as the first step of the CDP-choline pathway for the biosynthesis of phosphatidylcholine, has been recognized as a new target for anticancer therapy. Crystal structures of human choline kinase in its apo, ADP and phosphocholine-bound complexes, respectively, reveal the molecular details of the substrate binding sites. ATP binds in a cavity where residues from both the N and C-terminal lobes contribute to form a cleft, while the choline-binding site constitutes a deep hydrophobic groove in the C-terminal domain with a rim composed of negatively charged residues. Upon binding of choline, the enzyme undergoes conformational changes independently affecting the N-terminal domain and the ATP-binding loop. From this structural analysis and comparison with other kinases, and from mutagenesis data on the homologous Caenorhabditis elegans choline kinase, a model of the ternary ADP.phosphocholine complex was built that reveals the molecular basis for the phosphoryl transfer activity of this enzyme.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17007874}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17007874 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17007874}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Phosphatydilcholine]] | | [[Category: Phosphatydilcholine]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:22:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:22:16 2008'' |
