Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-8-10
pubmed:databankReference
pubmed:abstractText
Structural comparisons of the two GTPase activating proteins (GAPs) p120 and p50 in complex with Ras and Rho, respectively, allowed us to decipher the functional role of specific structural features, such as helix alpha8c of p120 and helix A1 of p50, necessary for small GTPase recognition. We identified important residues that may be critical for stabilization of the GAP/GTPase binary complexes. Detection of topohydrophobic positions (positions which are most often occupied by hydrophobic amino acids within a family of protein domains) conserved between the two GAP families led to the characterization of a common flexible four-helix bundle. Altogether, these data are consistent with a rearrangement of several helices around a common core, which strongly supports the assumption that p50 and p120 GAPs derive from a unique fold. Considered as a whole, the remarkable plasticity of GAPs appears to be a means used by nature to accurately confer functional specificity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
477
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-105
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10899318-Amino Acid Sequence, pubmed-meshheading:10899318-Binding Sites, pubmed-meshheading:10899318-Conserved Sequence, pubmed-meshheading:10899318-Crystallography, X-Ray, pubmed-meshheading:10899318-GTPase-Activating Proteins, pubmed-meshheading:10899318-Models, Molecular, pubmed-meshheading:10899318-Molecular Sequence Data, pubmed-meshheading:10899318-Pliability, pubmed-meshheading:10899318-Protein Binding, pubmed-meshheading:10899318-Protein Structure, Secondary, pubmed-meshheading:10899318-Protein Structure, Tertiary, pubmed-meshheading:10899318-Sequence Alignment, pubmed-meshheading:10899318-Substrate Specificity, pubmed-meshheading:10899318-p120 GTPase Activating Protein, pubmed-meshheading:10899318-ras Proteins, pubmed-meshheading:10899318-rho GTP-Binding Proteins
pubmed:year
2000
pubmed:articleTitle
Functional specificity conferred by the unique plasticity of fully alpha-helical Ras and Rho GAPs.
pubmed:affiliation
SmithKline Beecham Laboratoires Pharmaceutiques, 4 rue Chesnay- Beauregard, 35760 Saint-Grégiure, France.
pubmed:publicationType
Journal Article, Comparative Study