1B55

PH DOMAIN FROM BRUTON'S TYROSINE KINASE IN COMPLEX WITH INOSITOL 1,3,4,5-TETRAKISPHOSPHATE

1B55 の概要

• エントリーDOI: 10.2210/pdb1b55/pdb
• 分子名称: TYROSINE-PROTEIN KINASE BTK, ZINC ION, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: transferase, ph domain, btk motif, zinc binding, x-linked agammaglobulinemia, tyrosine-protein kinase, inositol 1, 3, 4, 5-tetrakisphosphate
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q06187
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41097.00

構造登録者

Djinovic Carugo, K.,Baraldi, E.,Hyvoenen, M.,Lo Surdo, P.,Riley, A.M.,Potter, B.V.L.,O'Brien, R.,Ladbury, J.E.,Saraste, M. (登録日: 1999-01-12, 公開日: 1999-06-15, 最終更新日: 2024-05-22)

主引用文献

Baraldi, E.,Djinovic Carugo, K.,Hyvonen, M.,Surdo, P.L.,Riley, A.M.,Potter, B.V.,O'Brien, R.,Ladbury, J.E.,Saraste, M.
Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate.
Structure Fold.Des., 7:449-460, 1999

PubMed Abstract: The activity of Bruton's tyrosine kinase (Btk) is important for the maturation of B cells. A variety of point mutations in this enzyme result in a severe human immunodeficiency known as X-linked agammaglobulinemia (XLA). Btk contains a pleckstrin-homology (PH) domain that specifically binds phosphatidylinositol 3,4,5-trisphosphate and, hence, responds to signalling via phosphatidylinositol 3-kinase. Point mutations in the PH domain might abolish membrane binding, preventing signalling via Btk.

PubMed: 10196129
DOI: 10.1016/S0969-2126(99)80057-4

実験手法

X-RAY DIFFRACTION (2.4 Å)