1zm0 | pdb_00001zm0

Crystal Structure of the Carboxyl Terminal PH Domain of Pleckstrin To 2.1 Angstroms

spinqualitylabelsall models 1zm0, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1zm0 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1xxo Gene: PLEK, P47 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PLEK_HUMAN] Major protein kinase C substrate of platelets. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed. Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms.,Jackson SG, Zhang Y, Bao X, Zhang K, Summerfield R, Haslam RJ, Junop MS Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):324-30. Epub 2006, Feb 22. PMID:16510979 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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