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Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_hal_primary_oai_HAL_hal_02349772v1

Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

About this item

Full title

Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

Publisher

Washington, DC: American Association for the Advancement of Science

Journal title

Science (American Association for the Advancement of Science), 2003-10, Vol.302 (5645), p.646-650

Language

English

Formats

Publication information

Publisher

Washington, DC: American Association for the Advancement of Science

More information

Scope and Contents

Contents

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....

Alternative Titles

Full title

Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_hal_primary_oai_HAL_hal_02349772v1

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_hal_primary_oai_HAL_hal_02349772v1

Other Identifiers

ISSN

0036-8075

E-ISSN

1095-9203

DOI

10.1126/science.1087761