Protein kinase Spk1

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**[[1fhr]], [[1j4k]], [[1j4l]], [[1k2m]], [[1k2n]] – yRad53 + Rad9 peptide - NMR<br />
**[[1fhr]], [[1j4k]], [[1j4l]], [[1k2m]], [[1k2n]] – yRad53 + Rad9 peptide - NMR<br />
-
*Rad53 kinase and SCD2 domains
+
*Rad53 kinase and SCD2 domains residues 170-512
**[[4pdp]] – yRad53 kinase and SCD2 domain (mutant)<br />
**[[4pdp]] – yRad53 kinase and SCD2 domain (mutant)<br />
**[[4pds]] – yRad53 kinase and SCD2 domain (mutant) + AMPPNP<br />
**[[4pds]] – yRad53 kinase and SCD2 domain (mutant) + AMPPNP<br />
 +
 +
*Rad53 residues 1-466
 +
 +
**[[5xzw]] – yRad53 <br />
 +
**[[5xzv]] – yRad53 + AMPPNP<br />
 +
}}
}}

Revision as of 07:32, 29 August 2018

Structure of yeast Rad53 FHA1 domain (cyan) complex with phosphothreonine peptide (green) (PDB code 1k3n).

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3D structures of protein kinase Spk1

Updated on 29-August-2018

References

  1. Stern DF, Zheng P, Beidler DR, Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Mol Cell Biol. 1991 Feb;11(2):987-1001. PMID:1899289
  2. Yuan C, Yongkiettrakul S, Byeon IJ, Zhou S, Tsai MD. Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. J Mol Biol. 2001 Nov 30;314(3):563-75. PMID:11846567 doi:10.1006/jmbi.2001.5140

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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