Lee, JK Moon, T Chi, MW Song, JS Choi, YS Yoon, CN 2024-01-21T08:38:33Z 2024-01-21T08:38:33Z 2021-09-03 2003-06-20 0006-291X https://pubs.kist.re.kr/handle/201004/138456 A comparative molecular field analysis (CoMFA) was carried out to investigate quantitative structure-activity relationships for SH2-binding phosphopeptides. Two alignment rules were applied in our CoMFA model. The phosphopeptide backbone atoms were used for superposition in alignment I and the backbone atoms of peptide-binding residues of SH2-phosphopeptide complexes were used in alignment II to consider the position of phosphopeptides in SH2-binding sites. The higher correlation and predictivity in alignment II (r(2) value of 0.961 and cross-validated r(2) value of 0.682) suggest that the consideration of peptide-binding position at the binding sites gives rise to better results when the ligand-receptor complex structure is considered. In addition, CoMFA contour and electrostatic maps were well accorded with the experimental results in which the replacement of N-terminal residues with an acetyl group reduced the binding affinity. Therefore, the modification of molecular size and charge of phosphopeptides can be carried out based on these contour maps in order to increase binding affinities. (C) 2003 Elsevier Science (USA). All rights reserved. English ACADEMIC PRESS INC ELSEVIER SCIENCE AFFINITY PHOSPHOTYROSYL PEPTIDE SIGNAL TRANSDUCTION CRYSTAL-STRUCTURES PROTEIN-KINASE RECOGNITION PP60C-SRC P56(LCK) FAMILY An investigation of phosphopeptide binding to SH2 domain Article 10.1016/S0006-291X(03)00932-X 1 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.306, no.1, pp.225 - 230 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 306 1 225 230 scie scopus 000183676900036 2-s2.0-0038730721 Biochemistry & Molecular Biology Biophysics Biochemistry & Molecular Biology Biophysics Article AFFINITY PHOSPHOTYROSYL PEPTIDE SIGNAL TRANSDUCTION CRYSTAL-STRUCTURES PROTEIN-KINASE RECOGNITION PP60C-SRC P56(LCK) FAMILY QSAR CoMFA SH2 phosphopeptides binding affinity alignment rule