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Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Å

✍ Scribed by Jackson, S. G. ;Zhang, Y. ;Bao, X. ;Zhang, K. ;Summerfield, R. ;Haslam, R. J. ;Junop, M. S.

Book ID
104478188
Publisher
International Union of Crystallography
Year
2006
Tongue
English
Weight
672 KB
Volume
62
Category
Article
ISSN
0907-4449

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✦ Synopsis

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.

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