Premium
Characterization of a novel zinc binding site of protein kinase C inhibitor‐1
Author(s) -
Mozier Ned M.,
Walsh Michael P.,
Pearson James D.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80238-x
Subject(s) - zinc , binding site , chemistry , dissociation constant , nitrocellulose , histidine , biochemistry , protein kinase a , stereochemistry , kinase , enzyme , membrane , receptor , organic chemistry
The zinc‐binding properties of an endogenous protein inhibitor of protein kinase C was studied. Equilibrium gel penetration revealed that 1 mol of this protein binds 0.97 mol of zinc with a dissociation constant of 4.3 μM. The site of zinc‐binding. MVVNEGSDGGQSVYHVHLHVLGGR, was indentified by a multi‐step process consisting of tryptic digestion, fragment isolation, transfer to nitrocellulose, and hybridization with 65 ZnCl 2 . Binding of 65 ZnCl 2 to selected synthetic fragments further localized the site of interaction to the sequence QSVYHVHLHVL. This region contains 3 closely positioned histidine residues and represent a novel zinc‐binding site.