1YRK

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

Summary for 1YRK

Entry DOI	10.2210/pdb1yrk/pdb
Related	1BDY
Descriptor	Protein kinase C, delta type, 13-residue peptide, ACETIC ACID, ... (4 entities in total)
Functional Keywords	c2 domain, protein binding
Biological source	Homo sapiens (human) More
Cellular location	Cytoplasm (By similarity): Q05655
Total number of polymer chains	2
Total formula weight	15993.29
Authors	Benes, C.H.,Wu, N.,Elia, A.E.,Dharia, T.,Cantley, L.C.,Soltoff, S.P. (deposition date: 2005-02-03, release date: 2005-07-26, Last modification date: 2011-07-13)
Primary citation	Benes, C.H.,Wu, N.,Elia, A.E.,Dharia, T.,Cantley, L.C.,Soltoff, S.P. The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell(Cambridge,Mass.), 121:271-280, 2005 Cited by PubMed Abstract: 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. PubMed: 15851022 DOI: 10.1016/j.cell.2005.02.019 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation