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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1990-12-13
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pubmed:abstractText |
Residues 370-383 (helix C) of the human nerve growth factor receptor (NGF-R) are highly similar to the sequence of the 14 residue wasp toxin, mastoparan. Both regions are predicted to form amphiphilic alpha-helices, as is the amino-terminal region of the third intracytoplasmic loop (i3) of the beta 2-adrenergic receptor (beta 2AR). As both mastoparan and the beta 2AR i3 interact with G-proteins, it is suggested that helix C of the NGF-R may facilitate interactions with a cytoplasmic protein. A similar structural motif was identified in the cytoplasmic domains of a number of other growth factor receptors, suggesting an important role for this motif in signal transduction mechanisms.
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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 |
Oct
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pubmed:issn |
0014-5793
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2172020-Amino Acid Sequence,
pubmed-meshheading:2172020-GTP-Binding Proteins,
pubmed-meshheading:2172020-Humans,
pubmed-meshheading:2172020-Molecular Sequence Data,
pubmed-meshheading:2172020-Peptides,
pubmed-meshheading:2172020-Protein Conformation,
pubmed-meshheading:2172020-Receptors, Adrenergic, beta,
pubmed-meshheading:2172020-Receptors, Somatotropin,
pubmed-meshheading:2172020-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2172020-Wasp Venoms
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pubmed:year |
1990
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pubmed:articleTitle |
Identification of a conserved protein motif in a group of growth factor receptors.
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pubmed:affiliation |
Institut de Physiologie, Faculté de Médicine, Université de Lausanne, Switzerland.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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