1AWO

THE SOLUTION NMR STRUCTURE OF ABL SH3 AND ITS RELATIONSHIP TO SH2 IN THE SH(32) CONSTRUCT, 20 STRUCTURES

Summary for 1AWO

• Entry DOI: 10.2210/pdb1awo/pdb
• Descriptor: ABL TYROSINE KINASE (1 entity in total)
• Functional Keywords: kinase, sh3 domain, transferase, phosphotransferase, proto-oncogene, multiple domain, leukemia
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519
• Total number of polymer chains: 1
• Total formula weight: 6637.30

Authors

Cowburn, D. (deposition date: 1997-10-03, release date: 1998-01-28, Last modification date: 2024-05-22)

Primary citation

Gosser, Y.Q.,Zheng, J.,Overduin, M.,Mayer, B.J.,Cowburn, D.
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
Structure, 3:1075-1086, 1995

PubMed Abstract: The Src homology domains, SH3 and SH2, of Abl protein tyrosine kinase regulate enzymatic activity in vivo. Abl SH3 suppresses kinase activity, whereas Abl SH2 is required for the transforming activity of the activated form of Abl. We expect that the solution structures of Abl SH3, Abl SH2 and Abl SH(32) (a dual domain comprising SH3 and SH2 subdomains) will contribute to a structural basis for understanding the mechanism of the Abl 'regulatory apparatus'.

PubMed: 8590002
DOI: 10.1016/S0969-2126(01)00243-X

Experimental method

SOLUTION NMR