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Tham khảo luận văn - đề án 'báo cáo khoa học: s100–annexin complexes – structural insights', luận văn - báo cáo, báo cáo khoa học phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | REVIEW ARTICLE S100-annexin complexes - structural insights Anne C. Rintala-Dempsey Atoosa Rezvanpour and Gary S. Shaw Department of Biochemistry University of Western Ontario London Canada Keywords calcium-binding protein didalcin EF-hand membrane interaction NMR spectroscopy protein interaction S100A11 S100B structure X-ray crystallography Correspondence G. S. Shaw Department of Biochemistry University of Western Ontario London ON N6A 5C1 Canada Fax 1 519 661 3175 Tel 1 519 661 4021 E-mail gshaw1@uwo.ca Received 16 June 2008 revised 29 July 2008 accepted 5 August 2008 doi 10.1111 j.1742-4658.2008.06654.x Annexins and S100 proteins represent two large but distinct calcium-binding protein families. Annexins are made up of a highly a-helical core domain that binds calcium ions allowing them to interact with phospholipid membranes. Furthermore some annexins such as annexins A1 and A2 contain an N-terminal region that is expelled from the core domain on calcium binding. These events allow for the interaction of the annexin N-terminus with target proteins such as S100. In addition when an S100 protein binds calcium ions it undergoes a structural reorientation of its helices exposing a hydrophobic patch capable of interacting with its targets including the N-terminal sequences of annexins. Structural studies of the complexes between members of these two families have revealed valuable details regarding the mechanisms of the interactions including the binding surfaces and conformation of the annexin N-termi-nus. However other S100-annexin interactions such as those between S100A11 and annexin A6 or between dicalcin and annexins A1 A2 and A5 appear to be more complicated involving the annexin core region perhaps in concert with the N-terminus. The diversity of these interactions indicates that multiple forms of recognition exist between S100 proteins and annexins. S100-annexin interactions have been suggested to play a role in membrane fusion events by the bridging .
