Structure of the pleckstrin homology domain from β-spectrin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-06

AUTHORS

Maria J. Macias, Andrea Musacchio, Hannes Ponstingl, Michael Nilges, Matti Saraste, Hartmut Oschkinat

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 factors1–4. Its function is not known, but many proteins that contain a PH domain interact with GTP-binding proteins5. The PH domain in β-adrenergic receptor kinase may be involved in binding to the βγ subunits of a trimeric G-protein3, 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 β-sheet consisting of seven strands. The C terminus is folded into a long α-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). More... »

PAGES

675-677

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/369675a0

DOI

http://dx.doi.org/10.1038/369675a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044438856

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8208297


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