3B2W

Crystal structure of pyrimidine amide 11 bound to Lck

Summary for 3B2W

• Entry DOI: 10.2210/pdb3b2w/pdb
• Related: 2OFV
• Descriptor: Proto-oncogene tyrosine-protein kinase LCK, N-[5-({[2-fluoro-3-(trifluoromethyl)phenyl]amino}carbonyl)-2-methylphenyl]-4-methoxy-2-[(4-piperazin-1-ylphenyl)amino]pyrimidine-5-carboxamide (3 entities in total)
• Functional Keywords: lck, kinase domain, alternative splicing, atp-binding, chromosomal rearrangement, cytoplasm, disease mutation, host-virus interaction, lipoprotein, membrane, myristate, nucleotide-binding, palmitate, phosphorylation, proto-oncogene, sh2 domain, sh3 domain, transferase, tyrosine-protein kinase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P06239
• Total number of polymer chains: 1
• Total formula weight: 32682.26

Authors

Huang, X. (deposition date: 2007-10-19, release date: 2007-12-18, Last modification date: 2023-08-30)

Primary citation

Deak, H.L.,Newcomb, J.R.,Nunes, J.J.,Boucher, C.,Cheng, A.C.,DiMauro, E.F.,Epstein, L.F.,Gallant, P.,Hodous, B.L.,Huang, X.,Lee, J.H.,Patel, V.F.,Schneider, S.,Turci, S.M.,Zhu, X.
N-(3-(phenylcarbamoyl)arylpyrimidine)-5-carboxamides as potent and selective inhibitors of Lck: structure, synthesis and SAR.
Bioorg.Med.Chem.Lett., 18:1172-1176, 2008

PubMed Abstract: N-3-(Phenylcarbamoyl)arylpyrimidine-5-carboxamides are a novel class of selective Lck inhibitors. This series of compounds derives its selectivity from a hydrogen bond with the gatekeeper Thr316 of the enzyme. X-ray co-crystal structural data, structure-activity relationships, and the synthesis of these inhibitors are reported herein.

PubMed: 18083554
DOI: 10.1016/j.bmcl.2007.11.123

Experimental method

X-RAY DIFFRACTION (2.3 Å)