1B55

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

Summary for 1B55

• Entry DOI: 10.2210/pdb1b55/pdb
• Descriptor: TYROSINE-PROTEIN KINASE BTK, ZINC ION, INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transferase, ph domain, btk motif, zinc binding, x-linked agammaglobulinemia, tyrosine-protein kinase, inositol 1, 3, 4, 5-tetrakisphosphate
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q06187
• Total number of polymer chains: 2
• Total formula weight: 41097.00

Authors

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. (deposition date: 1999-01-12, release date: 1999-06-15, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)