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rdf:type |
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lifeskim:mentions |
umls-concept:C0018353,
umls-concept:C0079471,
umls-concept:C0205177,
umls-concept:C0242853,
umls-concept:C0243071,
umls-concept:C0249197,
umls-concept:C0288472,
umls-concept:C0376315,
umls-concept:C0439855,
umls-concept:C0444626,
umls-concept:C0600499,
umls-concept:C1420626
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pubmed:issue |
12
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pubmed:dateCreated |
1990-7-19
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pubmed:abstractText |
Normal RAS proteins play a key role of molecular switch in the transduction of the growth signal from extracellular to intracellular space. The state of the switch is "on" when GTP is bound and "off" when GDP is bound to the protein. The crystal structure of a complex between a nonhydrolyzable GTP analog and the catalytic domain of a RAS protein has been determined by a rotation-translation search method. The orientations and positions of four independent molecules have been determined using a single molecule as a probe in the search. The crystal structure reveals that the gamma phosphate of the GTP analog induces extensive conformational changes on two loop regions of the protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2329580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2406906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2425352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2448879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2476675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2539374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2642607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2665078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2821624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-2842690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-3082814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-3103658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-3113327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-3201259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-3304147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-361078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-4079798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2191303-6365920
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4849-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2191303-Amino Acid Sequence,
pubmed-meshheading:2191303-Binding Sites,
pubmed-meshheading:2191303-Cloning, Molecular,
pubmed-meshheading:2191303-Crystallization,
pubmed-meshheading:2191303-Escherichia coli,
pubmed-meshheading:2191303-Guanosine Triphosphate,
pubmed-meshheading:2191303-Models, Molecular,
pubmed-meshheading:2191303-Molecular Sequence Data,
pubmed-meshheading:2191303-Protein Binding,
pubmed-meshheading:2191303-Protein Conformation,
pubmed-meshheading:2191303-Protein-Tyrosine Kinases,
pubmed-meshheading:2191303-Proto-Oncogene Proteins,
pubmed-meshheading:2191303-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:2191303-Recombinant Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.
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pubmed:affiliation |
Howard Hughes Medical Institute, Yale University, New Haven, CT 06511.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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