Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2008-4-9
pubmed:abstractText
The GTP-binding protein Rap1 regulates integrin-mediated and other cell adhesion processes. Unlike most other Ras-related proteins, it contains a threonine in switch II instead of a glutamine (Gln61 in Ras), a residue crucial for the GTPase reaction of most G proteins. Furthermore, unlike most other GTPase-activating proteins (GAPs) for small G proteins, which supply a catalytically important Arg-finger, no arginine residue of RapGAP makes a significant contribution to the GTPase reaction of Rap1. For a detailed understanding of the reaction mechanism, we have solved the structure of Rap1 in complex with Rap1GAP. It shows that the Thr61 of Rap is away from the active site and that an invariant asparagine of RapGAPs, the Asn-thumb, takes over the role of the cis-glutamine of Ras, Rho or Ran. The structure and biochemical data allow to further explain the mechanism and to define the important role of a conserved tyrosine. The structure and biochemical data furthermore show that the RapGAP homologous region of the tumour suppressor Tuberin is sufficient for catalysis on Rheb.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-10222271, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-11331911, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-11701921, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-11812780, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-11832950, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12239560, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12460576, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12771962, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12820960, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12869586, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12906785, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-12963376, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-14607972, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-15141215, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-15299926, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-15340059, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-15562827, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-15728574, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-16431904, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-16511497, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-16763562, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-16807243, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-16855591, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-17300802, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-17540168, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-8710841, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-8756332, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9219684, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9302992, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9312017, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9338791, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9757107, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9846874, http://linkedlifedata.com/resource/pubmed/commentcorrection/18309292-9893994
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1460-2075
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1145-53
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues.
pubmed:affiliation
Department of Structural Biology, Max-Planck-Institute of Molecular Physiology, Dortmund, Germany.
pubmed:publicationType
Journal Article