1SHF

CRYSTAL STRUCTURE OF THE SH3 DOMAIN IN HUMAN FYN; COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SH3 DOMAINS IN TYROSINE KINASES AND SPECTRIN

1SHF の概要

• エントリーDOI: 10.2210/pdb1shf/pdb
• 分子名称: FYN TYROSINE KINASE SH3 DOMAIN (1 entity in total)
• 機能のキーワード: phosphotransferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13476.57

構造登録者

Noble, M.,Musacchio, A.,Saraste, M.,Wierenga, R. (登録日: 1993-05-19, 公開日: 1993-10-31, 最終更新日: 2024-02-14)

主引用文献

Noble, M.E.,Musacchio, A.,Saraste, M.,Courtneidge, S.A.,Wierenga, R.K.
Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
EMBO J., 12:2617-2624, 1993

PubMed Abstract: The Src-homology 3 (SH3) region is a protein domain consisting of approximately 60 residues. It occurs in a large number of eukaryotic proteins involved in signal transduction, cell polarization and membrane--cytoskeleton interactions. The function is unknown, but it is probably involved in specific protein--protein interactions. Here we report the crystal structure of the SH3 domain of Fyn (a Src family tyrosine kinase) at 1.9 A resolution. The crystals have two SH3 molecules per asymmetric unit. These two Fyn SH3 domains are not related by a local twofold axis. The crystal structures of spectrin and Fyn SH3 domains as well as the solution structure of the Src SH3 domain show that these all have the same basic fold. A protein domain which has the same topology as SH3 is present in the prokaryotic regulatory enzyme BirA. The comparison between the crystal structures of Fyn and spectrin SH3 domains shows that a conserved surface patch, consisting mainly of aromatic residues, is flanked by two hairpin-like loops (residues 94-104 and 114-118 in Fyn). These loops are different in tyrosine kinase and spectrin SH3 domains. They could modulate the binding properties of the aromatic surface.

PubMed: 7687536

実験手法

X-RAY DIFFRACTION (1.9 Å)