title: Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms.
abstract: 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.
authors.affiliation: Department of Biochemistry and Biomedical Sciences, McMaster University, Canada.
authors.forename: S G
authors.initials: SG
authors.lastname: Jackson
authors.forename: Y
authors.initials: Y
authors.lastname: Zhang
authors.forename: X
authors.initials: X
authors.lastname: Bao
authors.forename: K
authors.initials: K
authors.lastname: Zhang
authors.forename: R
authors.initials: R
authors.lastname: Summerfield
authors.forename: R J
authors.initials: RJ
authors.lastname: Haslam
authors.forename: M S
authors.initials: MS
authors.lastname: Junop
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D004268:DNA-Binding Proteins; D008024:Ligands; D010716:Phosphatidylinositols