TAILIEUCHUNG - Báo cáo khoa học: Natural and amyloid self-assembly of S100 proteins: structural basis of functional diversity

The S100 proteins are 10–12 kDa EF-hand proteins that act as central reg-ulators in a multitude of cellular processes including cell survival, prolifera-tion, differentiation and motility. Consequently, many S100 proteins are implicated and display marked changes in their expression levels in many types of cancer, neurodegenerative disorders, inflammatory and autoim-mune diseases. | MINIREVIEW Natural and amyloid self-assembly of S100 proteins structural basis of functional diversity Gunter Fritz1 Hugo M. Botelho2 Ludmilla A. Morozova-Roche3 and Claudio M. Gomes2 1 Department of Neuropathology University of Freiburg Germany 2 Instituto de Tecnologia Quimica e Biologica Universidade Nova de Lisboa Oeiras Portugal 3 Department of MedicalBiochemistry and Biophysics Umea University Sweden Keywords amyloid fibril function metal ions misfolding oligomer self-assembly structure S100 proteins Correspondence C. M. Gomes Instituto de Tecnologia Química e Biológica Universidade Nova de Lisboa Oeiras Portugal Fax 351 214 411 277 Tel 351 214 469 332 E-mail gomes@ L. A. Morozova-Roche Department of MedicalBiochemistry and Biophysics Umea University Umea Sweden Fax 46 90 786 9795 Tel 46 90 786 5283 E-mail . Received 27 May 2010 revised 2 August 2010 accepted 18 August 2010 doi The S100 proteins are 10-12 kDa EF-hand proteins that act as central regulators in a multitude of cellular processes including cell survival proliferation differentiation and motility. Consequently many S100 proteins are implicated and display marked changes in their expression levels in many types of cancer neurodegenerative disorders inflammatory and autoimmune diseases. The structure and function of S100 proteins are modulated by metal ions via Ca2 binding through EF-hand motifs and binding of Zn2 and Cu2 at additional sites usually at the homodimer interfaces. Ca2 binding modulates S100 conformational opening and thus promotes and affects the interaction with p53 the receptor for advanced glycation endproducts and Toll-like receptor 4 among many others. Structural plasticity also occurs at the quaternary level where several S100 proteins selfassemble into multiple oligomeric states many being functionally relevant. Recently we have found that the S100A8 A9 proteins are involved in amy-loidogenic .

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