1QPJ

CRYSTAL STRUCTURE OF THE LYMPHOCYTE-SPECIFIC KINASE LCK IN COMPLEX WITH STAUROSPORINE.

Summary for 1QPJ

• Entry DOI: 10.2210/pdb1qpj/pdb
• Related: 1QPC 1QPD 1QPE
• Descriptor: LCK TYROSINE KINASE, SULFATE ION, STAUROSPORINE, ... (4 entities in total)
• Functional Keywords: alpha beta fold, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P06239
• Total number of polymer chains: 1
• Total formula weight: 32916.41

Authors

Zhu, X.,Kim, J.L.,Rose, P.E.,Stover, D.R.,Toledo, L.M. (deposition date: 1999-05-25, release date: 2000-05-31, Last modification date: 2024-10-30)

Primary citation

Zhu, X.,Kim, J.L.,Newcomb, J.R.,Rose, P.E.,Stover, D.R.,Toledo, L.M.,Zhao, H.,Morgenstern, K.A.
Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors.
Structure Fold.Des., 7:651-661, 1999

PubMed Abstract: The lymphocyte-specific kinase Lck is a member of the Src family of non-receptor tyrosine kinases. Lck catalyzes the initial phosphorylation of T-cell receptor components that is necessary for signal transduction and T-cell activation. On the basis of both biochemical and genetic studies, Lck is considered an attractive cell-specific target for the design of novel T-cell immunosuppressants. To date, the lack of detailed structural information on the mode of inhibitor binding to Lck has limited the discovery of novel Lck inhibitors.

PubMed: 10404594
DOI: 10.1016/S0969-2126(99)80086-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)