1DYN

CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM HUMAN DYNAMIN

1DYN の概要

• エントリーDOI: 10.2210/pdb1dyn/pdb
• 分子名称: DYNAMIN (2 entities in total)
• 機能のキーワード: signal transduction protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q05193
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29467.45

構造登録者

Ferguson, K.M.,Lemmon, M.A.,Schlessinger, J.,Sigler, P.B. (登録日: 1994-12-21, 公開日: 1995-02-27, 最終更新日: 2024-02-07)

主引用文献

Ferguson, K.M.,Lemmon, M.A.,Schlessinger, J.,Sigler, P.B.
Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin.
Cell(Cambridge,Mass.), 79:199-209, 1994

PubMed Abstract: The X-ray crystal structure of the pleckstrin homology (PH) domain from human dynamin has been refined to 2.2 A resolution. A seven-stranded beta sandwich of two orthogonal antiparallel beta sheets is closed at one corner by a C-terminal alpha helix. Opposite this helix are the three loops that vary most among PH domains. The basic fold is very similar to that of two other PH domains recently determined by nuclear magnetic resonance, confirming that PH domain with known structure is electrostatically polarized, with the three variable loops forming a positively charged surface. This surface includes the position of the X-linked immunodeficiency mutation in the Btk PH domain and may serve as a ligand-binding surface.

PubMed: 7954789
DOI: 10.1016/0092-8674(94)90190-2

実験手法

X-RAY DIFFRACTION (2.2 Å)