Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease.

Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Research Abstract Details 

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Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Abstract Text:

H Kawasaki,Y Emori,S Imajoh-Ohmi,Y Minami,K Suzuki,

We reported previously the cDNA cloning of the endogenous inhibitor for calcium-dependent protease (CANP inhibitor, calpastatin) and the expression of its fragments in Escherichia coli. The CANP inhibitor has four internal repeating domains each spanning about 140 amino acid residues. The inhibitory activity arises from these domains which have a well-conserved sequence, TIPPXYR, in their central positions. The inhibitory activities of various fragments expressed in E. coli suggest the involvement of the regions around the well-conserved sequences. In this report, we describe further detailed investigation on the interaction site of the CANP inhibitor with CANP by truncating inhibitor fragments and by using chemically synthesized peptides. The results clearly indicate that the sequence around the well-conserved sequence, TIPPXYR, is an interaction site. A peptide as short as 23 amino acid residues retained inhibitory activity, but a 9-residue peptide corresponding to the conserved sequence, VTIPPKYRE had none. The inhibitory sequence is suggested as LGXKDREXTIPPXYRXLL. The analysis of the competition between an inhibitor peptide and an irreversible inhibitor, E-64 for the reaction with the active site suggests no involvement of the active site cysteine residue of CANP in the inhibitory interaction between CANP and the CANP inhibitor. The high specificity of the CANP inhibitor to CANP arises from its interaction with residues other than the active site cysteine residue, possibly the subsite for substrate-binding of CANP.

Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Publishing Authors By Initials

H Kawasaki,Y Emori,S Imajoh-Ohmi,Y Minami,K Suzuki,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: base sequence: repetitive sequences, nucleic acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: base sequence: repetitive sequences, nucleic acid research

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Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 106

Page Numbers: 274-81

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1989

Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Keywords Mesh Terms:

KEYWORDS: Repetitive Sequences, Nucleic Acid

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. Information

Substance Name: Calpain

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease.

AFFILIATION: Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science.

Country: JAPAN

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MEDLINETA: J Biochem

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