2HSP

SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA

「1HSP」から置き換えられました

2HSP の概要

• エントリーDOI: 10.2210/pdb2hsp/pdb
• 分子名称: PHOSPHOLIPASE C-GAMMA (SH3 DOMAIN) (1 entity in total)
• 機能のキーワード: phosphoric diester hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell projection, lamellipodium: P19174
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8249.24

構造登録者

Kohda, D.,Hatanaka, H.,Odaka, M.,Inagaki, F. (登録日: 1994-06-13, 公開日: 1994-08-31, 最終更新日: 2024-05-01)

主引用文献

Kohda, D.,Hatanaka, H.,Odaka, M.,Mandiyan, V.,Ullrich, A.,Schlessinger, J.,Inagaki, F.
Solution structure of the SH3 domain of phospholipase C-gamma.
Cell(Cambridge,Mass.), 72:953-960, 1993

PubMed Abstract: SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-gamma (PLC-gamma) was determined by two-dimensional 1H NMR analysis. This SH3 domain is composed of eight antiparallel beta strands consisting of two successive "Greek key" motifs, which form a barrel-like structure. The conserved aliphatic and aromatic residues form a hydrophobic pocket on the molecular surface, and the conserved carboxylic residues are localized to the periphery. The hydrophobic pocket may serve as a binding site for target proteins. Analysis of the slowly exchanging amide protons by NMR measurements indicates that despite containing a high content of beta structure, the SH3 domain of PLC-gamma is flexible.

PubMed: 7681365
DOI: 10.1016/0092-8674(93)90583-C

実験手法

SOLUTION NMR