CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA-2 IN COMPLEX WITH ADP

File:2ckp.gif


2ckp, resolution 3.10Å

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OverviewOverview

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, ... [(full description)]

About this StructureAbout this Structure

2CKP is a [Single protein] structure of sequence from [Homo sapiens] with ADP as [ligand]. Active as [Choline kinase], with EC number [2.7.1.32]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine., Malito E, Sekulic N, Too WC, Konrad M, Lavie A, J Mol Biol. 2006 Nov 24;364(2):136-51. Epub 2006 Sep 3. PMID:17007874

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