1QWE

C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND APP12

1QWE の概要

• エントリーDOI: 10.2210/pdb1qwe/pdb
• 分子名称: TYROSINE-PROTEIN KINASE TRANSFORMING PROTEIN SRC, ALA-PRO-PRO-LEU-PRO-PRO-ARG-ASN-ARG-PRO-ARG-LEU (2 entities in total)
• 機能のキーワード: src sh3 domain, class ii ligand complex, complex (signal transduction-peptide) complex, complex (signal transduction/peptide)
• 由来する生物種: Avian sarcoma virus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8491.42

構造登録者

Feng, S.,Chiyoshi, K.,Rickles, R.J.,Schreiber, S.L. (登録日: 1995-11-09, 公開日: 1996-03-08, 最終更新日: 2024-05-22)

主引用文献

Feng, S.,Kasahara, C.,Rickles, R.J.,Schreiber, S.L.
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands.
Proc.Natl.Acad.Sci.USA, 92:12408-12415, 1995

PubMed Abstract: Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity.

PubMed: 8618911
DOI: 10.1073/pnas.92.26.12408

実験手法

SOLUTION NMR