TAILIEUCHUNG - Báo cáo khoa học: Aplysia temptin ) the ‘glue’ in the water-borne attractin pheromone complex

Temptin, a component of the complex of water-borne protein pheromones that stimulate attraction and mating behavior in the marine mollusk Aply-sia, has sequence homology to the epidermal growth factor (EGF)-like domains of higher organisms that mediate protein–cell surface contact dur-ing fertilization and blood coagulation. | ỊFEBS Journal Aplysia temptin - the glue in the water-borne attractin pheromone complex Scott F. Cummins1 2 Fang Xie3 Melissa R. de Vries1 Suresh P. Annangudi3 Milind Misra4 Bernard M. Degnan2 Jonathan V. Sweedler3 Gregg T. Nagle1 and Catherine H. Schein4 5 1 Department of Neuroscience and CellBiology University of Texas MedicalBranch Galveston TX USA 2 Schoolof Integrative Biology University of Queensland St Lucia Australia 3 Department of Chemistry and the Beckman Institute University of Illinois at Urbana-Champaign Urbana IL USA 4 Sealy Center for StructuralBiology Department of Biochemistry and Molecular Biology Sealy Center for Vaccine Design University of Texas MedicalBranch Galveston TX USA 5 Department of Microbiology and Immunology Sealy Center for Vaccine Design University of Texas MedicalBranch Galveston TX USA Keywords enticin fibrillin epidermalgrowth factor-like domains Marfan s syndrome signaling network Correspondence C. H. Schein 218 Clay Hall Department of Biochemistry and Molecular Biology UTMB Galveston TX 77555-0857 USA Fax 1 409 747 6000 Tel 1 409 747 6843 E-mail chschein@ Received 29 June 2007 revised 15 August 2007 accepted 28 August 2007 doi Temptin a component of the complex of water-borne protein pheromones that stimulate attraction and mating behavior in the marine mollusk Aply-sia has sequence homology to the epidermal growth factor EGF -like domains of higher organisms that mediate protein-cell surface contact during fertilization and blood coagulation. In this work recombinant temptin for structural and functional studies was produced in Escherichia coli using a cold shock promoter and purified by RP-HPLC. CD spectra confirmed a predominantly b-sheet structure. Two disulfide bonds were determined via limited proteolysis and MS. One internal disulfide Cys57-Cys77 was predicted from initial alignments with class I EGF-like domains the second between Cys18 and Cys103 could protect temptin against

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