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Article

Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase.

Science (New York, N.Y.) - 24 Oct 2003

Rak Alexey, Pylypenko Olena, Durek Thomas, Watzke Anja, Kushnir Susanna, Brunsveld Lucas, Waldmann Herbert, Goody Roger S, Alexandrov Kirill

Abstract excerpt

Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution...

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Identifiers

PMID: 14576435
DOI: 10.1126/science.1087761

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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