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1yrk

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1yrk, resolution 1.70Å ()
Ligands:
Non-Standard Residues:
Related: 1bdy
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

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

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1yrk is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

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Reference

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