Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
In this issue of Cell, report that the C2 domain of the serine/threonine protein kinase Cdelta is a phosphotyrosine binding domain and present the crystal structure of this C2 domain bound to a peptide containing phosphotyrosine. Prior to this work, C2 domains were thought to bind only to phospholipids or to unphosphorylated proteins, and the SH2 and PTB domains were the only signaling domains known to recognize phosphotyrosine. This new role for the C2 domain links phosphotyrosine recognition directly to serine/threonine kinase activity and reveals an unexpected mechanism for crosstalk between distinct signaling pathways.
C2 can do it, too.,Sondermann H, Kuriyan J Cell. 2005 Apr 22;121(2):158-60. PMID:15851022[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sondermann H, Kuriyan J. C2 can do it, too. Cell. 2005 Apr 22;121(2):158-60. PMID:15851022 doi:http://dx.doi.org/10.1016/j.cell.2005.04.001
