TAILIEUCHUNG - Báo cáo khoa học: Structural and functional characterization of human Iba proteins

Iba2 is a homolog of ionized calcium-binding adapter molecule 1 (Iba1), a 17-kDa protein that binds and cross-links filamentous actin (F-actin) and localizes to membrane ruffles and phagocytic cups. Here, we present the crystal structure of human Iba2 and its homodimerization properties, F-actin cross-linking activity, cellular localization and recruitment upon bacterial invasion in comparison with Iba1. | ỊFEBS Journal Structural and functional characterization of human Iba proteins Jorg O. Schulze1 Claudia Quedenau2 Yvette Roske1 Thomas Adam3 Herwig Schuler1 Joachim Behlke1 Andrew P. Turnbull1 Volker Sievert2 Christoph Scheich2 Uwe Mueller4 Udo Heinemann1 5 and Konrad Bussow2 6 1 Max Delbruck Center for Molecular Medicine Berlin Germany 2 Max Planck Institute for Molecular Genetics Berlin Germany 3 Institute of Microbiology and Hygiene Charites MedicalSchool Berlin Germany 4 Macromolecular Crystallography BESSY GmbH Berlin Germany 5 Institute of Chemistry and Biochemistry - Crystallography Free University Berlin Germany 6 Department of StructuralBiology Helmholtz Centre for Infection Research Braunschweig Germany Keywords actin cross-linking allograft inflammatory factor 1 calcium binding EF-hand ionized calcium binding adapter molecule Correspondence U. Heinemann MDC Robert-Rossle-Str. 10 13125 Berlin Germany Fax 49 30 9406 2548 Tel 49 30 9406 3420 E-mail heinemann@ Database The coordinates of both structures have been deposited in the RCSB Protein Data Bank under PDB codes 2vtg and 2jjz Received 20 March 2008 revised 18 July 2008 accepted 22 July 2008 doi Iba2 is a homolog of ionized calcium-binding adapter molecule 1 Ibal a 17-kDa protein that binds and cross-links filamentous actin F-actin and localizes to membrane ruffles and phagocytic cups. Here we present the crystal structure of human Iba2 and its homodimerization properties F-actin cross-linking activity cellular localization and recruitment upon bacterial invasion in comparison with Iba1. The Iba2 structure comprises two central EF-hand motifs lacking bound Ca2 . Iba2 crystallized as a homodimer stabilized by a disulfide bridge and zinc ions. Analytical ultracentrifugation revealed a different mode of dimerization under reducing conditions that was independent of Ca2 . Furthermore no binding of Ca2 up to mM was detected by equilibrium dialysis. .

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