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Mechanism of the activation of proteinase inhibitor synthesis by systemin involves beta-sheet structure, a specific DNA-binding protein domain

Slósarek, G. and Kalbitzer, Hans Robert and Mucha, P. and Rekowski, P. and Kupryszewski, G. and Giel-Pietraszuk, M. and Szymański, M. and Barciszewski, J. (1995) Mechanism of the activation of proteinase inhibitor synthesis by systemin involves beta-sheet structure, a specific DNA-binding protein domain. Journal of structural biology 115 (1), pp. 30-36.

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Abstract

We analyzed a tertiary structure of systemin, the first identified polypeptide plant hormone, using two-dimensional NMR spectroscopy. From these data and molecular dynamics calculations we concluded that the peptide can adopt a Z-like-beta-sheet structure, which has previously been found in many specific DNA-binding proteins. Using DNA-cellulose affinity chromatography, we showed that systemin ...

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Item Type:Article
Date:1995
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
7577230PubMed ID
10.1006/jsbi.1995.1026DOI
Classification:
NotationType
Amino Acid SequenceMESH
Base SequenceMESH
Chromatography, AffinityMESH
Computer GraphicsMESH
DNA/metabolismMESH
DNA-Binding Proteins/metabolismMESH
Gene Expression Regulation, PlantMESH
Lactoferrin/metabolismMESH
Lycopersicon esculentum/chemistryMESH
Magnetic Resonance SpectroscopyMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Peptide Fragments/metabolismMESH
Peptides/pharmacologyMESH
Plant Proteins/pharmacologyMESH
Protease Inhibitors/metabolismMESH
Protein FoldingMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:09 Sep 2010 06:57
Last Modified:09 Sep 2010 06:57
Item ID:16540
Owner Only: item control page
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