Protein kinase Spk1
From Proteopedia
(Difference between revisions)
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *Rad53 FHA1 domain | + | *Rad53 FHA1 domain 1-164 |
**[[1k3j]] – yRad53 – yeast - NMR<br /> | **[[1k3j]] – yRad53 – yeast - NMR<br /> | ||
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**[[5t2f]] - yRad53/DBF4 BRCT domain<br /> | **[[5t2f]] - yRad53/DBF4 BRCT domain<br /> | ||
**[[5t2s]] - yRad53/DBF4 BRCT domain + phosphopeptide<br /> | **[[5t2s]] - yRad53/DBF4 BRCT domain + phosphopeptide<br /> | ||
| - | *Rad53 FHA2 domain | + | |
| + | *Rad53 FHA2 domain 573-730 | ||
**[[1qu5]], [[1dmz]], [[1fhq]] – yRad53 – yeast - NMR<br /> | **[[1qu5]], [[1dmz]], [[1fhq]] – yRad53 – yeast - NMR<br /> | ||
Current revision
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3D structures of protein kinase Spk1
Updated on 03-February-2022
References
- ↑ 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
- ↑ 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
