Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-1-25
pubmed:abstractText
A truncated human c-Ha-Ras protein that lacks the C-terminal 18 amino acid residues and the truncated Ras protein with the amino acid substitution Gly-->Val in position 12 were prepared by an E. coli overexpression system. The truncated Ras protein showed the same guanine-nucleotide binding activity and GTPase activity as those of the full-length Ras protein. Further, the same extent of GTPase activity enhancement due to GTPase-activating protein was observed for the truncated and full-length Ras proteins. In fact, two-dimensional proton NMR analyses indicated that the tertiary structure of the truncated Ras protein (GDP-bound or GMPPNP-bound) was nearly the same as that of the corresponding catalytic domain of the full-length Ras protein. Moreover, a conformational change around the effector region upon GDP-->GMPPNP exchange occurred in the same manner for both proteins. These observations indicate that the C-terminal flanking region (18 amino acid residues) of the Ras protein does not appreciably interact with the catalytic domain. Therefore, the truncated Ras protein is suitable for studying the molecular mechanism involved in the GTPase activity and the interaction with the GTPase-activating protein. On the other hand, an active form of the truncated Ras protein, unlike that of the full-length Ras protein, did not induce neurite outgrowth of rat pheochromocytoma PC12 cells. Thus, membrane anchoring of the Ras protein through its C-terminal four residues is not required for the interaction of Ras and GAP, but may be essential for the following binding of the Ras-GAP complex with the putative downstream target.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanylyl Imidodiphosphate, http://linkedlifedata.com/resource/pubmed/chemical/HRAS protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins p21(ras), http://linkedlifedata.com/resource/pubmed/chemical/Solutions, http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0277-8033
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
731-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1466766-Animals, pubmed-meshheading:1466766-Binding Sites, pubmed-meshheading:1466766-Catalysis, pubmed-meshheading:1466766-GTP Phosphohydrolases, pubmed-meshheading:1466766-GTPase-Activating Proteins, pubmed-meshheading:1466766-Guanine Nucleotides, pubmed-meshheading:1466766-Guanosine Diphosphate, pubmed-meshheading:1466766-Guanosine Triphosphate, pubmed-meshheading:1466766-Guanylyl Imidodiphosphate, pubmed-meshheading:1466766-Humans, pubmed-meshheading:1466766-Magnetic Resonance Spectroscopy, pubmed-meshheading:1466766-Neurites, pubmed-meshheading:1466766-PC12 Cells, pubmed-meshheading:1466766-Protein Conformation, pubmed-meshheading:1466766-Proteins, pubmed-meshheading:1466766-Proto-Oncogene Proteins p21(ras), pubmed-meshheading:1466766-Rats, pubmed-meshheading:1466766-Signal Transduction, pubmed-meshheading:1466766-Solutions, pubmed-meshheading:1466766-ras GTPase-Activating Proteins
pubmed:year
1992
pubmed:articleTitle
Guanine-nucleotide binding activity, interaction with GTPase-activating protein and solution conformation of the human c-Ha-Ras protein catalytic domain are retained upon deletion of C-terminal 18 amino acid residues.
pubmed:affiliation
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't