NMR identification of calcineurin B residues affected by binding of a calcineurin A peptide.

Anglister, J; Ren, H; Klee, C B; Bax, A

Anglister, J; Ren, H; Klee, C B; Bax, A.

Affiliation

Anglister J; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.

FEBS Lett ; 375(1-2): 108-12, 1995 Nov 13.

Article in En | MEDLINE | ID: mdl-7498455

Subject(s)

Calcium-Binding Proteins/chemistry; Calcium-Binding Proteins/metabolism; Calmodulin-Binding Proteins/metabolism; Peptide Fragments/metabolism; Phosphoprotein Phosphatases/metabolism; Protein Conformation; Amino Acid Sequence; Binding Sites; Calcineurin; Calcium/metabolism; Calmodulin-Binding Proteins/chemistry; Cholic Acids; Detergents; Kinetics; Magnetic Resonance Spectroscopy/methods; Molecular Sequence Data; Peptide Fragments/chemical synthesis; Peptide Fragments/chemistry; Phosphoprotein Phosphatases/chemistry; Protein Structure, Secondary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Solubility

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Collection: 01-internacional Database: MEDLINE Main subject: Peptide Fragments / Protein Conformation / Calmodulin-Binding Proteins / Calcium-Binding Proteins / Phosphoprotein Phosphatases Type of study: Diagnostic_studies / Prognostic_studies Language: En Journal: FEBS Lett Year: 1995 Document type: Article Affiliation country: United States Country of publication: United kingdom

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