TAILIEUCHUNG - Báo cáo khoa học: Conserved structural determinants in three-fingered protein domains

The three-dimensional structures of some components of snake venoms forming so-called ‘three-fingered protein’ domains (TFPDs) are similar to those of the ectodomains of activin, bone morphogenetic protein and trans-forming growth factor-breceptors, and to a variety of proteins encoded by the Ly6andPlaurgenes. | ỊFEBS Journal Conserved structural determinants in three-fingered protein domains Andrzej Galat1 Gregory Gross2 Pascal Drevet2 Atsushi Sato3 and Andre Menez4 1 Institut de Biologie et de Technologies de Saclay SIMOPRO DSV CEA Gif-sur-Yvette France 2 Institut de Biologie et de Technologies de Saclay SBIGeM DSV CEA Gif-sur-Yvette France 3 Department of Information Science Faculty of LiberalArts Tohoku-Gakuin University Sendai Japan 4 Museum Nationald Histoire Naturelle Paris France Keywords atomic interactions cystine networks three-finger proteins three-fingered protein threefingered protein domain Correspondence A. Galat Bat. 152 CE-Saclay F-91191 Gif-sur-Yvette Cedex France Fax 33 1 69 08 90 71 Tel 33 1 69 08 84 67 E-mail galat@ Deceased. The former President of the Museum of NaturalHistory Paris France Received 6 March 2008 revised 17 April 2008 accepted 18 April 2008 doi The three-dimensional structures of some components of snake venoms forming so-called three-fingered protein domains TFPDs are similar to those of the ectodomains of activin bone morphogenetic protein and transforming growth factor-b receptors and to a variety of proteins encoded by the Ly6 and Plaur genes. The analysis of sequences of diverse snake toxins various ectodomains of the receptors that bind activin and other cytokines and numerous gene products encoded by the Ly6 and Plaur families of genes has revealed that they differ considerably from each other. The sequences of TFPDs may consist of up to six disulfide bonds three of which have the same highly conserved topology. These three disulfide bridges and an asparagine residue in the C-terminal part of TFPDs are essential for the TFPD-like fold. Analyses of the three-dimensional structures of diverse TFPDs have revealed that the three highly conserved disulfides impose a major stabilizing contribution to the TFPD-like fold in both TFPDs contained in some snake venoms and ectodomains of several

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