Linked Life Data

21795785

Source:http://linkedlifedata.com/resource/pubmed/id/21795785

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 7
pubmed:dateCreated
2011-7-28
pubmed:databankReference
pubmed:abstractText
Rab6 is a small GTPase that belongs to the p21 Ras superfamily. It is involved in vesicle trafficking between the Golgi apparatus and endosomes/ER in eukaryotes. The GDP-bound inactive protein undergoes conformational changes when the nucleotide is exchanged to GTP, allowing Rab6 to interact with a variety of different effector proteins. To further understand how these changes affect downstream protein binding, the crystal structure of Rab6 from Drosophila melanogaster has been solved to 1.4?Å resolution, the highest resolution for a Rab6 structure to date. The crystals belonged to space group C2, with unit-cell parameters a=116.5, b=42.71, c=86.86?Å, ?=90, ?=133.12, ?=90°. The model was refined to an R factor of 14.5% and an Rfree of 17.3%.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
744-8
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Structure of the Drosophila melanogaster Rab6 GTPase at 1.4?Å resolution.
pubmed:affiliation
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, England.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't