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.
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[[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>taylor1991</cite>.
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<biblio>
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#taylor1991 pmid=1862342
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</biblio>

Revision as of 18:35, 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].

  1. Knighton DR, Zheng JH, Ten Eyck LF, Ashford VA, Xuong NH, Taylor SS, and Sowadski JM. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science. 1991 Jul 26;253(5018):407-14. DOI:10.1126/science.1862342 | PubMed ID:1862342 | HubMed [taylor1991]