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Journal Article

STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN

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Citation

MACIAS, M., MUSACCHIO, A., PONSTINGL, H., NILGES, M., SARASTE, M., & OSCHKINAT, H. (1994). STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN. NATURE, 369(6482), 675-677. doi:10.1038/369675a0.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-7B90-8
Abstract
The 'pleckstrin homology' or PH domain is a 100-residue protein module. It is present in many kinases, different isoforms of phospholipase C, GTPase-activating proteins and nucleotide-exchange factors(1-4). Its function is not known, but many proteins that contain a PH domain interact with GTP-binding proteins(5). The PH domain in beta-adrenergic receptor kinase may be involved in binding to the beta gamma subunits of a trimeric G-protein(3,4,6,7). We report here the three-dimensional structure of the PH domain of the cytoskeletal protein spectrin using homonuclear nuclear magnetic resonance. The core of the molecule is an antiparallel beta-sheet consisting of seven strands. The C terminus is folded into a long alpha-helix, and another helix is present in one of the surface loops. The molecule is electrostatically polarized and contains a pocket which may be involved in the binding of a ligand. There is a distant relationship to the peptidyl-prolyl-cis-trans-isomerase FKBP in which this pocket is involved in the binding of the macrocyclic compound FK506 (refs 8-11).