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  STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM BETA-SPECTRIN

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.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-0015-7B90-8 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-0015-7B91-6
Genre: Zeitschriftenartikel

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 Urheber:
MACIAS, MJ1, Autor
MUSACCHIO, A1, Autor
PONSTINGL, H1, Autor
NILGES, M1, Autor
SARASTE, M1, Autor
OSCHKINAT, H1, Autor
Affiliations:
1external, ou_persistent22              

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Schlagwörter: -
 Zusammenfassung: 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).

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Sprache(n):
 Datum: 1994
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: A1994NT45900063
DOI: 10.1038/369675a0
 Art des Abschluß: -

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Titel: NATURE
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 369 (6482) Artikelnummer: - Start- / Endseite: 675 - 677 Identifikator: ISSN: 0028-0836