Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-4-21
pubmed:abstractText
The two cysteines C494 and C569, located in the first and second extracellular loop, respectively, of the thyrotropin (TSH) receptor, were mutated to serines to test the functional significance of the putative disulfide bond between these two cysteines. Single (C494S and C569S) and double (C494/569S) mutant receptors were generated, transiently expressed in COS cells, and compared with regard to the ability to bind ligand and to mediate stimulation of adenylate cyclase activity. The double mutant retained ligand binding capacity, in contrast to the single cysteine mutants that were essentially devoid of binding capacity. The ability of the mutated receptor variants to stimulate adenylate cyclase activity was lost or greatly reduced.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
199
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
612-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8135801-Adenylate Cyclase, pubmed-meshheading:8135801-Adult, pubmed-meshheading:8135801-Amino Acid Sequence, pubmed-meshheading:8135801-Animals, pubmed-meshheading:8135801-Base Sequence, pubmed-meshheading:8135801-Binding, Competitive, pubmed-meshheading:8135801-Binding Sites, pubmed-meshheading:8135801-Cell Line, pubmed-meshheading:8135801-Cyclic AMP, pubmed-meshheading:8135801-Cysteine, pubmed-meshheading:8135801-Gene Library, pubmed-meshheading:8135801-Genetic Variation, pubmed-meshheading:8135801-Graves Disease, pubmed-meshheading:8135801-Humans, pubmed-meshheading:8135801-Kinetics, pubmed-meshheading:8135801-Molecular Sequence Data, pubmed-meshheading:8135801-Mutagenesis, Site-Directed, pubmed-meshheading:8135801-Oligodeoxyribonucleotides, pubmed-meshheading:8135801-Point Mutation, pubmed-meshheading:8135801-Protein Structure, Secondary, pubmed-meshheading:8135801-Receptors, Thyrotropin, pubmed-meshheading:8135801-Serine, pubmed-meshheading:8135801-Thyroid Gland, pubmed-meshheading:8135801-Thyrotropin, pubmed-meshheading:8135801-Transfection
pubmed:year
1994
pubmed:articleTitle
Point mutations of the thyrotropin receptor determining structural requirements for its ability to bind thyrotropin and to stimulate adenylate cyclase activity.
pubmed:affiliation
Department of Pathology, University Hospital, Uppsala, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't