TAILIEUCHUNG - Báo cáo khoa học: Serpins 2005 – fun between theb-sheets Meeting report based upon presentations made at the 4th Interna-tional Symposium on Serpin Structure, Function and Biology (Cairns, Australia)

Serpins are the largest family of protease inhibitors and are fundamental for the control of proteolysis in multicellular eukaryotes. Most eukaryote serpins inhibit serine or cysteine proteases, however, noninhibitory mem-bers have been identified that perform diverse functions in processes such as hormone delivery and tumour metastasis. More recently inhibitory ser-pins have been identified in prokaryotes and unicellular eukaryotes, never-theless, the precise molecular targets of these molecules remains to be identified | iFEBS Journal REVIEW ARTICLE Serpins 2005 - fun between the 0-sheets Meeting report based upon presentations made at the 4th International Symposium on Serpin Structure Function and Biology Cairns Australia James C. Whisstock1 2 3 Stephen P. Bottomley1 Phillip I. Bird1 Robert N. Pike1 and Paul Coughlin4 1 The Department of Biochemistry and Molecular Biology 2 ARC Centre for Structuraland FunctionalMicrobialGenomics and 3 Victorian Bioinformatics Consortium Monash University Clayton Campus Melbourne Victoria Australia 4 Australian Centre for Blood Diseases Monash University Prahran Victoria Australia Keywords conformational disease protease serpin serpinopathies Correspondence J. Whisstock Department of Biochemistry and Molecular Biology Monash University Clayton Victoria 3800 Australia E-mail Received 26 July 2005 revised 16 August 2005 accepted 18 August 2005 doi Serpins are the largest family of protease inhibitors and are fundamental for the control of proteolysis in multicellular eukaryotes. Most eukaryote serpins inhibit serine or cysteine proteases however noninhibitory members have been identified that perform diverse functions in processes such as hormone delivery and tumour metastasis. More recently inhibitory ser-pins have been identified in prokaryotes and unicellular eukaryotes nevertheless the precise molecular targets of these molecules remains to be identified. The serpin mechanism of protease inhibition is unusual and involves a major conformational rearrangement of the molecule concomitant with a distortion of the target protease. As a result of this requirement serpins are susceptible to mutations that result in polymerization and conformational diseases such as the human serpinopathies. This review reports on recent major discoveries in the serpin field based upon presentations made at the 4th International Symposium on Serpin Structure Function and Biology Cairns Australia . .

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