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      The Transcriptional Activity of NF-κB Is Regulated by the IκB-Associated PKAc Subunit through a Cyclic AMP–Independent Mechanism

      , , , ,

      Cell

      Elsevier BV

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          Most cited references 19

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          Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation.

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            The regulation of AP-1 activity by mitogen-activated protein kinases.

             M Karin (1995)
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              Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.

              The crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase complexed with a 20-amino acid substrate analog inhibitor has been solved and partially refined at 2.7 A resolution to an R factor of 0.212. The magnesium adenosine triphosphate (MgATP) binding site was located by difference Fourier synthesis. The enzyme structure is bilobal with a deep cleft between the lobes. The cleft is filled by MgATP and a portion of the inhibitor peptide. The smaller lobe, consisting mostly of amino-terminal sequence, is associated with nucleotide binding, and its largely antiparallel beta sheet architecture constitutes an unusual nucleotide binding motif. The larger lobe is dominated by helical structure with a single beta sheet at the domain interface. This lobe is primarily involved in peptide binding and catalysis. Residues 40 through 280 constitute a conserved catalytic core that is shared by more than 100 protein kinases. Most of the invariant amino acids in this conserved catalytic core are clustered at the sites of nucleotide binding and catalysis.
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                Author and article information

                Journal
                Cell
                Cell
                Elsevier BV
                00928674
                May 1997
                May 1997
                : 89
                : 3
                : 413-424
                Article
                10.1016/S0092-8674(00)80222-6
                © 1997

                http://www.elsevier.com/tdm/userlicense/1.0/

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