Difference between revisions of "K72"
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[[Kinase Glossary]]: [[K72]] | [[Kinase Glossary]]: [[K72]] | ||
| − | [[K72]] is a key conserved residue in [[ePK]] and most [[PKL]] kinases. It is part of the VAIK motif in the b3 strand. This lysine hydrogen bonds to the alpha oxygen and the beta phosphate of ATP, stabilizing its negative charge, and also forms a salt bridge with [[E91]]. It is one of three residues (along with [[D166]] and [[D184]]) whose absence is used to predict [[pseudokinases]]. In the Wnk family of kinases, K72 is absent, but a similar lysine is seen close to the [[G-rich loop]] and performs the same function. The number 72 is based on the position of this residue in the first PKA kinase crystal <cite> | + | [[K72]] is a key conserved residue in [[ePK]] and most [[PKL]] kinases. It is part of the VAIK motif in the b3 strand. This lysine hydrogen bonds to the alpha oxygen and the beta phosphate of ATP, stabilizing its negative charge, and also forms a salt bridge with [[E91]]. It is one of three residues (along with [[D166]] and [[D184]]) whose absence is used to predict [[pseudokinases]]. In the Wnk family of kinases, K72 is absent, but a similar lysine is seen close to the [[G-rich loop]] and performs the same function. The number 72 is based on the position of this residue in the first PKA kinase crystal <cite>taylor1993</cite>. |
<biblio> | <biblio> | ||
| − | # | + | #taylor1993 pmid=15299527 |
</biblio> | </biblio> | ||
Latest revision as of 21:05, 13 May 2014
Kinase Glossary: K72
K72 is a key conserved residue in ePK and most PKL kinases. It is part of the VAIK motif in the b3 strand. This lysine hydrogen bonds to the alpha oxygen and the beta phosphate of ATP, stabilizing its negative charge, and also forms a salt bridge with E91. It is one of three residues (along with D166 and D184) whose absence is used to predict pseudokinases. In the Wnk family of kinases, K72 is absent, but a similar lysine is seen close to the G-rich loop and performs the same function. The number 72 is based on the position of this residue in the first PKA kinase crystal [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 |
