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. 2005 Apr 22;121(2):271-80.
doi: 10.1016/j.cell.2005.02.019.

The C2 domain of PKCdelta is a phosphotyrosine binding domain

Cyril H Benes  1 , Ning Wu, Andrew E H Elia, Tejal Dharia, Lewis C Cantley, Stephen P Soltoff
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Free article

The C2 domain of PKCdelta is a phosphotyrosine binding domain

Cyril H Benes et al. Cell. .
Free article

Abstract

In eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recognizing phosphotyrosine residues on target proteins. Here we make the unexpected finding that the C2 domain of PKCdelta directly binds to phosphotyrosine peptides in a sequence-specific manner. We provide evidence that this domain mediates PKCdelta interaction with a Src binding glycoprotein, CDCP1. The crystal structure of the PKCdelta C2 domain in complex with an optimal phosphopeptide reveals a new mode of phosphotyrosine binding in which the phosphotyrosine moiety forms a ring-stacking interaction with a histidine residue of the C2 domain. This is also the first example of a protein Ser/Thr kinase containing a domain that binds phosphotyrosine.

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Comment in

  • C2 can do it, too.
    Sondermann H, Kuriyan J. Sondermann H, et al. Cell. 2005 Apr 22;121(2):158-60. doi: 10.1016/j.cell.2005.04.001. Cell. 2005. PMID: 15851022 Review.

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