English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN

MPS-Authors
There are no MPG-Authors in the publication available
External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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).