Linked Life Data

10360579

Source:http://linkedlifedata.com/resource/pubmed/id/10360579

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6734
pubmed:dateCreated
1999-6-16
pubmed:databankReference
pubmed:abstractText
The proteins Cdc42 and Rac are members of the Rho family of small GTPases (G proteins), which control signal-transduction pathways that lead to rearrangements of the cell cytoskeleton, cell differentiation and cell proliferation. They do so by binding to downstream effector proteins. Some of these, known as CRIB (for Cdc42/Rac interactive-binding) proteins, bind to both Cdc42 and Rac, such as the PAK1-3 serine/threonine kinases, whereas others are specific for Cdc42, such as the ACK tyrosine kinases and the Wiscott-Aldrich-syndrome proteins (WASPs). The effector loop of Cdc42 and Rac (comprising residues 30-40, also called switch I), is one of two regions which change conformation on exchange of GDP for GTP. This region is almost identical in Cdc42 and Racs, indicating that it does not determine the specificity of these G proteins. Here we report the solution structure of the complex of Cdc42 with the GTPase-binding domain ofACK. Both proteins undergo significant conformational changes on binding, to form a new type of G-protein/effector complex. The interaction extends the beta-sheet in Cdc42 by binding an extended strand from ACK, as seen in Ras/effector interactions, but it also involves other regions of the G protein that are important for determining the specificity of effector binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
399
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
384-8
pubmed:dateRevised
2011-7-4
pubmed:meshHeading
pubmed-meshheading:10360579-Amino Acid Sequence, pubmed-meshheading:10360579-Cell Cycle Proteins, pubmed-meshheading:10360579-Conserved Sequence, pubmed-meshheading:10360579-Escherichia coli, pubmed-meshheading:10360579-GTP Phosphohydrolases, pubmed-meshheading:10360579-GTP-Binding Proteins, pubmed-meshheading:10360579-Humans, pubmed-meshheading:10360579-Magnetic Resonance Spectroscopy, pubmed-meshheading:10360579-Models, Molecular, pubmed-meshheading:10360579-Molecular Sequence Data, pubmed-meshheading:10360579-Protein Binding, pubmed-meshheading:10360579-Protein Conformation, pubmed-meshheading:10360579-Protein-Tyrosine Kinases, pubmed-meshheading:10360579-Recombinant Fusion Proteins, pubmed-meshheading:10360579-Sequence Homology, Amino Acid, pubmed-meshheading:10360579-cdc42 GTP-Binding Protein
pubmed:year
1999
pubmed:articleTitle
Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK.
pubmed:affiliation
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't