2I5F

Crystal structure of the C-terminal PH domain of pleckstrin in complex with D-myo-Ins(1,2,3,5,6)P5

Summary for 2I5F

• Entry DOI: 10.2210/pdb2i5f/pdb
• Related: 1ZM0 2I5C
• Descriptor: Pleckstrin, (1R,2R,3R,4R,5S,6S)-6-HYDROXYCYCLOHEXANE-1,2,3,4,5-PENTAYL PENTAKIS[DIHYDROGEN (PHOSPHATE)] (3 entities in total)
• Functional Keywords: ph domain, protein-inositol phosphate complex, lipid binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 13031.22

Authors

Jackson, S.G.,Haslam, R.J.,Junop, M.S. (deposition date: 2006-08-24, release date: 2007-08-07, Last modification date: 2024-02-21)

Primary citation

Jackson, S.G.,Zhang, Y.,Haslam, R.J.,Junop, M.S.
Structural analysis of the carboxy terminal PH domain of pleckstrin bound to D-myo-inositol 1,2,3,5,6-pentakisphosphate.
Bmc Struct.Biol., 7:80-80, 2007

PubMed Abstract: Pleckstrin homology (PH) domains are one of the most prevalent domains in the human proteome and represent the major phosphoinositide-binding module. These domains are often found in signaling proteins and function predominately by targeting their host proteins to the cell membrane. Inositol phosphates, which are structurally similar to phosphoinositides, are not only known to play a role as signaling molecules but are also capable of being bound by PH domains.

PubMed: 18034889
DOI: 10.1186/1472-6807-7-80

Experimental method

X-RAY DIFFRACTION (1.35 Å)