Difference between revisions of "D166"
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| − | [[D166]] is a key conserved residue in [[ePK]] and most [[PKL]] kinases. It is known as the catalytic aspartate or catalytic base and is part of the catalytic loop motif HxDxxxxN. While the catalytic mechanism of protein kinases is not fully resolved, the side chain carboxyl group of D166 does hydrogen bond to the hydroxyl group of the substrate residue and facilitates phospho-transfer. It is one of three residues (along with [[K72]] and [[D184]]) whose absence is used to predict [[pseudokinases]]. The number 166 is based on the position of this residue in the first PKA kinase crystal, 1ATP. | + | [[D166]] is a key conserved residue in [[ePK]] and most [[PKL]] kinases. It is known as the catalytic aspartate or catalytic base and is part of the catalytic loop motif HxDxxxxN. While the catalytic mechanism of protein kinases is not fully resolved, the side chain carboxyl group of D166 does hydrogen bond to the hydroxyl group of the substrate residue and facilitates phospho-transfer. It is one of three residues (along with [[K72]] and [[D184]]) whose absence is used to predict [[pseudokinases]]. The number 166 is based on the position of this residue in the first PKA kinase crystal, 1ATP <cite>taylor1993</cite>. |
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| + | #taylor1993 pmid=15299527 | ||
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Latest revision as of 21:06, 13 May 2014
Kinase Glossary: D166
D166 is a key conserved residue in ePK and most PKL kinases. It is known as the catalytic aspartate or catalytic base and is part of the catalytic loop motif HxDxxxxN. While the catalytic mechanism of protein kinases is not fully resolved, the side chain carboxyl group of D166 does hydrogen bond to the hydroxyl group of the substrate residue and facilitates phospho-transfer. It is one of three residues (along with K72 and D184) whose absence is used to predict pseudokinases. The number 166 is based on the position of this residue in the first PKA kinase crystal, 1ATP [1].
- Zheng J, Trafny EA, Knighton DR, Xuong NH, Taylor SS, Ten Eyck LF, and Sowadski JM. 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr D Biol Crystallogr. 1993 May 1;49(Pt 3):362-5. DOI:10.1107/S0907444993000423 |
