TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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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.
Rab GTPases regulate membrane trafficking by cycling between inactive (GDP-bound) and active (GTP-bound) conformat...
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Full title
TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
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TN_cdi_proquest_miscellaneous_876247038
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_876247038
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ISSN
0028-0836
E-ISSN
1476-4687,1476-4679
DOI
10.1038/nature04847
