1yrk

The C2 Domain of PKC<delta> is a new Phospho-Tyrosine Binding DomainThe C2 Domain of PKC<delta> is a new Phospho-Tyrosine Binding Domain

Structural highlights

1yrk is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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

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OCA

[1] 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

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