tailieunhanh - Báo cáo khoa học: Functional aspects of the solution structure and dynamics of PAF – a highly-stable antifungal protein from Penicillium chrysogenum

Penicilliumantifungal protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candi-date against the often lethalAspergillusinfections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-protein coupled sig-nalling followed by apoptosis. | ỊFEBS Journal Functional aspects of the solution structure and dynamics of PAF - a highly-stable antifungal protein from Penicillium chrysogenum Gyula Batta1 Terez Barna1 Zoltán Gaspari2 Szabolcs Sandor1 Katalin E. Kover3 Ulrike Binder4 Rottina a m5 I H 19 lốa ICO ro r4 A n 11 K f h h 111 a r4 A nd 1 03 Rinontlot 4 C a I ai ot 6 M i ko lo ta I lonodiic6 Denina oaiy Dy Vila Ixaiseiei I III lx. Vr II11111 ai I i vnea Liyenuci L va Deiiei IXI ixoieLLa neyevius Istvan Pocsi6 Herbert Lindner5 and Florentine Marx4 1 Department of Biochemistry Centre of Arts Humanities and Sciences University of Debrecen Hungary 2 Institute of Chemistry Eotvos Lorand University Budapest Hungary 3 Department of Inorganic and Ana lytica l Chemistry Centre of Arts Humanities and Sciences University of Debrecen Hungary 4 Division of Mo l ecu l ar Bio logy Biocenter Innsbruck Medica l University Austria 5 Division of ClinicalBiochemistry Biocenter Innsbruck MedicalUniversity Austria 6 Department of MicrobialBiotechnology and CellBiology Centre of Arts Humanities and Sciences University of Debrecen Hungary Keywords antifungalprotein PAF internaldynamics NMR spectroscopy site-directed mutagenesis solution structure Correspondence G. Batta Department of Biochemistry Centre of Arts Humanities and Sciences University of Debrecen Egyetem tér 1 H-4010 Debrecen Hungary Fax 36 52 453836 Tel 36 52 512900 22234 E-mail batta@ F. Marx Division of Molecular Biology Biocenter Innsbruck Medical University Fritz-Pregl Strasse 3 A-6020 Innsbruck Austria Fax 43 512 9003 73100 Tel 43 512 9003 70207 E-mail Database The structuralensemble without disulfide bond constraints has been deposited in Research CollaboratoryforStructuralBioinformatics Protein Data Bank RCSB ID code rcsb100954 PDB IDcode 2kcn . NMR chemical shift assignments are deposited in the BioMagResBank with accession number 16087 Received 25 January 2009 revised 13 March 2009 accepted 18 March 2009 doi .