2PNI

SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE

2PNI の概要

• エントリーDOI: 10.2210/pdb2pni/pdb
• 分子名称: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN (1 entity in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9649.58

構造登録者

Booker, G.W.,Gout, I.,Downing, A.K.,Driscoll, P.C.,Boyd, J.,Waterfield, M.D.,Campbell, I.D. (登録日: 1993-07-19, 公開日: 1993-10-31, 最終更新日: 2024-05-01)

主引用文献

Booker, G.W.,Gout, I.,Downing, A.K.,Driscoll, P.C.,Boyd, J.,Waterfield, M.D.,Campbell, I.D.
Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase.
Cell(Cambridge,Mass.), 73:813-822, 1993

PubMed Abstract: SH3 domains are found in proteins associated with receptor tyrosine kinase signal transduction complexes. The solution structure of the SH3 domain of the 85 kd regulatory subunit of phosphatidylinositol 3-kinase is shown to be a compact beta barrel consisting of five beta strands arranged in two beta sheets of three and two strands. The structure is similar to that of chicken brain alpha spectrin but represents a distinct class of SH3 domain, with an insertion between the second and third beta strands that may influence binding specificity. 1H chemical shift changes induced by complex formation with a synthetic peptide derived from the SH3-binding protein dynamin, together with amino acid sequence comparisons, suggest that the ligand-binding site consists of a hydrophobic surface flanked by two charged loops.

PubMed: 7684655
DOI: 10.1016/0092-8674(93)90259-S

実験手法

SOLUTION NMR