1ZM0

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

Summary for 1ZM0

• Entry DOI: 10.2210/pdb1zm0/pdb
• Related: 1XXO
• Descriptor: Pleckstrin (2 entities in total)
• Functional Keywords: ph domain, beta sandwich, pleckstrin, lipid binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 26041.64

Authors

Jackson, S.G.,Zhang, Y.,Zhang, K.,Summerfield, R.,Haslam, R.J.,Junop, M.S. (deposition date: 2005-05-09, release date: 2006-02-28, Last modification date: 2024-02-14)

Primary citation

Jackson, S.G.,Zhang, Y.,Bao, X.,Zhang, K.,Summerfield, R.,Haslam, R.J.,Junop, M.S.
Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms.
Acta Crystallogr.,Sect.D, 62:324-330, 2006

PubMed 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.

PubMed: 16510979
DOI: 10.1107/S0907444905043179

Experimental method

X-RAY DIFFRACTION (2.1 Å)