TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism

Xiaojing Pan, Sudharshan Eathiraj, Mary Munson and David G. Lambright ()
Additional contact information
Xiaojing Pan: UMASS Medical School, Two Biotech
Sudharshan Eathiraj: UMASS Medical School, Two Biotech
Mary Munson: UMASS Medical School, Two Biotech
David G. Lambright: UMASS Medical School, Two Biotech

Nature, 2006, vol. 442, issue 7100, 303-306

Abstract: Structural insight into the complex between the GTPase Rab33 and the TBC domain of the GTPase-activating protein Gyp1p reveals that the TBC domain supplies two catalytic residues in trans — an unexpected dual finger mechanism.

Date: 2006
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature04847 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:442:y:2006:i:7100:d:10.1038_nature04847

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature04847

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().