TAILIEUCHUNG - Báo cáo khoa học: Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras

The troponin (Tn) complex is formed by TnC, TnI and TnT and is respon-sible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crys-tal structure of the core cardiac muscle troponin complex has been deter-mined, very little high resolution information is available regarding the skeletal muscle TnI–TnC complex. . | ềFEBS Journal Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras A n a f i Timli liiihira TqqÌp1 ỷ nctianH I p f l li oit a1 3 arloQ R Inr h I r1 4 I ri Q Tnrríaní1 3 Ml la w. Ilion Lju uica I doiu I lsiisuaiio L. r. J 11 vend waiios Dioci I JI Ills I uiiidi II Chuck S. Farah5 and Cdilos H. I. Ramos1 2 1 Centro de Biologia Molecular Estrutural Laboratorio Nacionalde Luz Sincrotron Brazil 2 Departamento de Bioquimica Instituto de Biologia Universidade Estadualde Campinas Brazil 3 Instituto de Fisica Universidade Estadualde Campinas Brazil 4 Laboratorio de Espectrometria de Massa Embrapa-Recursos Geneticos e Biotecnologia Brazil 5 Departamento de Bioquimica Instituto de Quimica Universidade de Sao Paulo Brazil Keywords troponin muscle contraction protein engineering limited proteolysis solution structure Correspondence . Ramos Centro de Biologia Molecular Estrutural Laboratorio Nacionalde Luz Sincrotron CP 6192 Campinas SP 13084971 Brazil Fax 55 19 3287 7110 Tel 55 19 3287 4520 E-mail cramos@ These authors contributed equally to this work. tPresent address Instituto de Quimica Universidade Estadual de Campinas Campinas SP Brazil Received 19 October 2004 revised 24 November 2004 accepted 6 December 2004 doi The troponin Tn complex is formed by TnC Tnl and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined very little high resolution information is available regarding the skeletal muscle Tnl-TnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains

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