Linked Life Data

7488212

Source:http://linkedlifedata.com/resource/pubmed/id/7488212

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-12-28
pubmed:abstractText
To determine which residues within the rat somatostatin receptor subtype SSTR2 may be interacting with the lys9 of somatostatin-14 (S-14), mutant SSTR2 receptors were created by mutating asp89 or asp122. [125I Tyr11]S-14 binding to D89A and D89E mutants suggests that asp89 is not directly involved in S-14 binding. Binding studies with the charge switch mutants, asp9S-14, and D122K, suggest that asp122 may be interacting with the lys9 of S-14. [125I Tyr11]asp9S-14 displayed saturable binding to D122K with an affinity comparable to that seen with [125I Tyr11]S-14 and WT SSTR2. These data suggest that the interaction between lys9 of S-14 and the TM3 asp122 of SSTR2 represents one contact site between S-14 and SSTR2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
216
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
913-21
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Identification of a critical aspartate residue in transmembrane domain three necessary for the binding of somatostatin to the somatostatin receptor SSTR2.
pubmed:affiliation
Department of Molecular and Cellular Biology, American Cyanamid Company, Princeton, NJ 08543-0400, USA.
pubmed:publicationType
Journal Article