TAILIEUCHUNG - Báo cáo khóa học: Structural properties of the protein SV-IV

We have investigated the molecular mechanisms that produce different structural and functional behavior in the monomeric and trimeric forms of seminal vesicle protein no. 4, a protein with immunomodulatory, anti-inflamma-tory, and procoagulant activity secreted from the rat seminal vesicle epithelium. The monomeric and trimeric forms were characterized in solution by CD. Details of the self-association process and structural changes that accompany aggregation were investigated by different experimental approaches: trypsin proteolysis, sequence analysis, chemical modification, and computer modeling | Eur. J. Biochem. 271 263-271 2004 FEBS 2003 doi Structural properties of the protein SV-IV Carlo Canorale1 Carla Caruso1 Giovanni Colonna2 3 Anaelo Facchiano4. Pasauale Ferranti4 5 Gianfranco Mamone4 Gianluca Picariello4 Flavia Colonna3 Salvatore Metafora6 and Paola Stiuso2 3 1 Dipartimento di Agrobiologia ed Agrochimica Universita. della Tuscia Viterbo Italy 2Dipartimento di Biochimica e Biofisica Seconda University Napoli Italy 3Centro di Ricerca Interdipartimentale di Scienze Computazionali e Biotecnologiche Napoli Italy 4Istituto di Scienze dell Alimentazione CNR Roma Italy 5Dipartimento di Scienza degli Alimenti Universita degli Studi di Napoli Federico II Italy 6Istituto Internazionale di Genetica e Biofisica CNR Napoli Italy We have investigated the molecular mechanisms that produce different structural and functional behavior in the monomeric and trimeric forms of seminal vesicle protein no. 4 a protein with immunomodulatory anti-inflammatory and procoagulant activity secreted from the rat seminal vesicle epithelium. The monomeric and trimeric forms were characterized in solution by CD. Details of the self-association process and structural changes that accompany aggregation were investigated by different experimental approaches trypsin proteolysis sequence analysis chemical modification and computer modeling. The self-association process induces conformational change mainly in the 1-70 region which appears to be without secondary structure in the monomer but contains a-helix in the trimer. In vivo proteolysis of seminal vesicle protein no. 4 generates active peptides and this is affected by the monomer trimer state which is regulated by the concentration of the protein. The information obtained shows how conformational changes between the monomeric and trimeric forms represent a crucial aspect of activity modulation. Keywords monomer proteolysis seminal vesicle protein SV-IV trimer. SV-IV seminal vesicle protein no. 4 .

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