JMS/Sandbox21

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The crystal structure for the tetromeric holoenzyme, [[3tnp]], supports the above observation. There is no interaction between <scene name='58/583419/Pka_dimer/3'>exon 1 residues</scene>, shown with halos, to the regulatory units, shown in green and purple.
The crystal structure for the tetromeric holoenzyme, [[3tnp]], supports the above observation. There is no interaction between <scene name='58/583419/Pka_dimer/3'>exon 1 residues</scene>, shown with halos, to the regulatory units, shown in green and purple.
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These three residues are also <scene name='58/583419/Pka_reg/3'>distant from PKI-interacting residues (halos and ball and stick)</scene> - a second regulator/inhibitor of the catalytic unit, as well.
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In addition, the exon 1 residues are also <scene name='58/583419/Pka_reg/3'>distant from PKI-interacting residues (halos and ball and stick)</scene> - a second regulator/inhibitor of the catalytic unit, as well. The exon 1 residues are distant from all regulatory units, both the pka regulator unit as well as the pki unit .
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This is also obvious from the pdb structure for the <scene name='58/583419/Pka_pki/1'>crystal of the catalytic unit bound to PKI (purple)</scene>, [[1atp]]<ref>PMID:15299527</ref>.
This is also obvious from the pdb structure for the <scene name='58/583419/Pka_pki/1'>crystal of the catalytic unit bound to PKI (purple)</scene>, [[1atp]]<ref>PMID:15299527</ref>.

Revision as of 17:33, 29 May 2016

PKA and Regulators

Caption for this structure

Drag the structure with the mouse to rotate

References

  1. Kim C, Xuong NH, Taylor SS. Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. Science. 2005 Feb 4;307(5710):690-6. PMID:15692043 doi:307/5710/690
  2. Zheng J, Trafny EA, Knighton DR, Xuong NH, Taylor SS, Ten Eyck LF, 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. PMID:15299527 doi:10.1107/S0907444993000423

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Joseph M. Steinberger

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