PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10455016-0 1999 Lysine mutagenesis identifies cationic charges of human CYP17 that interact with cytochrome b5 to promote male sex-hormone biosynthesis. Lysine 0-6 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 56-61 25315771-8 2014 The appositional surfaces include Lys-88, Arg-347, and Arg-358/Arg-449 of CYP17A1, which interact with Glu-61, Glu-42, and Glu-48/Glu-49 of b5, respectively. Lysine 34-37 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 74-81 19636199-4 2009 The molecular analysis of CYP17A1 revealed a novel homozygous missense mutation resulting in the substitution of arginine to lysine at the amino acid position 21 (p.R21L). Lysine 125-131 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 26-33 19040066-5 2008 RESULTS: The CYP17 genes of the patients were proved to hold a homozygous mutation with a base deletion and a base transversion (TAC/AA) in exon 6, which produced a missense mutation of Tyr-->Lys at codon 329 and changed the open reading frame following this codon. Lysine 195-198 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 13-18 10455016-5 1999 That the defect could be essentially reversed by lysine mutagenesis has led to the conclusion that the cationic charges on all three residues (at the positions of Arg(347), Arg(358), Arg(449)) are vital for the functional interaction of CYP17 with cytochrome b(5) and that the loss of any one of these cationic charges is catastrophic. Lysine 49-55 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 237-242