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2PL0

LCK bound to imatinib

Summary for 2PL0
Entry DOI10.2210/pdb2pl0/pdb
DescriptorProto-oncogene tyrosine-protein kinase LCK, 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE (3 entities in total)
Functional Keywordskinase phosphorylation, transferase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: P06239
Total number of polymer chains1
Total formula weight33892.70
Authors
Jacobs, M.D. (deposition date: 2007-04-18, release date: 2007-10-09, Last modification date: 2024-02-21)
Primary citationJacobs, M.D.,Caron, P.R.,Hare, B.J.
Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: Structure of lck/imatinib complex.
Proteins, 70:1451-1460, 2007
Cited by
PubMed Abstract: We report a clustering of public human protein kinase structures based on the conformations of two structural elements, the activation segment and the C-helix, revealing three discrete clusters. One cluster includes kinases in catalytically active conformations. Each of the other clusters contains a distinct inactive conformation. Typically, kinases adopt at most one of the inactive conformations in available X-ray structures, implying that one of the conformations is preferred for many kinases. The classification is consistent with selectivity profiles of several well-characterized kinase inhibitors. We show further that inhibitor selectivity profiles guide kinase classification. For example, selective inhibition of lck among src-family kinases by imatinib (Gleevec) suggests that the relative stabilities of inactive conformations of lck are different from other src-family kinases. We report the X-ray structure of the lck/imatinib complex, confirming that the conformation adopted by lck is distinct from other structurally-characterized src-family kinases and instead resembles kinases abl1 and kit in complex with imatinib. Our classification creates new paths for designing small-molecule inhibitors.
PubMed: 17910071
DOI: 10.1002/prot.21633
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

243083

数据于2025-10-15公开中

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