Binding affinity difference induced by the stereochemistry of the sulfoxide bridge of the cyclic peptide inhibitors of Grb2-SH2 domain: NMR studies for the structural origin

Biochemical and Biophysical Research Communications

Volumn 330, Issue 4, 2005, Pages 1254-1261

  Shi, Yan Hong ^a   Song, Yan Li ^a   Lin, Dong Hai ^a   Tan, Jinzhi ^a   Roller, Peter P ^b   Li, Qian ^a   Long, Ya Qiu ^a   Song, Guo Qiang ^a  

^a SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Chiral sulfoxide; Configuration; Cyclic peptide; Dynamics; Grb2 SH2 domain inhibitors; NMR; Signal transduction; Solution structure

Indexed keywords

ANTINEOPLASTIC AGENT; CARBON; GLUTAMIC ACID; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; LEUCINE; PROTEIN INHIBITOR; PROTEIN SH2; SULFOXIDE; TYROSINE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CHIRALITY; CONFORMATION; CONSENSUS SEQUENCE; CYCLIZATION; DIASTEREOISOMER; HYDROGEN BOND; HYDROPHILICITY; ISOMER; MOLECULAR DYNAMICS; MOLECULE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; PROTEIN TARGETING; SIMULATION; STEREOCHEMISTRY;

EID: 17044434658     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.03.110     Document Type: Article

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