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Structural insights into the function of the rab gdi superfamily

Academic Article
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Overview

authors

  • Wu, S. K.
  • Zeng, K.
  • Wilson, Ian
  • Balch, William E.

publication date

  • December 1996

journal

  • Trends in Biochemical Sciences  Journal

abstract

  • The 1.81 A crystal structure of Rab GDP-dissociation inhibitor (GDI), a protein that plays a critical role in the recycling of Rab GTPases involved in membrane vesicular transport, has been recently determined. Biochemical studies implicate a highly conserved region involved in Rab binding, which is common to both GDI and the evolutionarily-related choroideremia gene product (CHM/REP) required for Rab prenylation. Here, we summarize the mechanisms by which members of the GDI superfamily might function to coordinate events leading to membrane fusion, and we discuss the unexpected, yet striking structural homology of GDI to FAD-binding proteins.

subject areas

  • Adaptor Proteins, Signal Transducing
  • Alkyl and Aryl Transferases
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Carrier Proteins
  • Choroideremia
  • Conserved Sequence
  • Flavoproteins
  • GTP-Binding Proteins
  • Guanine Nucleotide Dissociation Inhibitors
  • Guanosine Diphosphate
  • Humans
  • Models, Molecular
  • Protein Conformation
  • rab GTP-Binding Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0968-0004

Digital Object Identifier (DOI)

  • 10.1016/s0968-0004(96)10062-1

PubMed ID

  • 9009830
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Additional Document Info

start page

  • 472

end page

  • 476

volume

  • 21

issue

  • 12

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