Source:http://linkedlifedata.com/resource/pubmed/id/10571147
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1999-12-23
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pubmed:abstractText |
A series of phosphopeptides containing alpha,alpha-disubstituted cyclic alpha-amino acids (Ac(n)c, 3 < or = n < or = 7; n refers to the number of carbons in the ring) at the X(+1) position of Ac-Tyr(PO3H2)-X(+1)-Asn-NH2 has been synthesised and their inhibitory activity as antagonists of the Grb2-SH2 domain has been determined in competitive binding assays. The SAR data obtained have been interpreted by using models constructed from the X-ray structure of the ligand-bound Grb2-SH2 domain. The used of alpha,alpha-disubstituted cyclic alpha-amino acids to map the binding pockets of proteins expands the classical alanine scan concept and takes advantage of the known conformational preferences of these amino acids.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2915-20
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:10571147-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10571147-Amino Acids, Cyclic,
pubmed-meshheading:10571147-Binding Sites,
pubmed-meshheading:10571147-GRB2 Adaptor Protein,
pubmed-meshheading:10571147-Models, Molecular,
pubmed-meshheading:10571147-Proteins,
pubmed-meshheading:10571147-src Homology Domains
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pubmed:year |
1999
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pubmed:articleTitle |
Mapping the X(+1) binding site of the Grb2-SH2 domain with alpha,alpha-disubstituted cyclic alpha-amino acids.
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pubmed:affiliation |
Novartis Pharma Inc., Oncology Research Department, Basel, Switzerland. carlos.garcia-echeverria@pharma.novartis.com
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pubmed:publicationType |
Journal Article
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