TAILIEUCHUNG - Báo cáo khoa học: Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C

Mature lung surfactant protein C (SP-C) corresponds to residues 24–58 of the 21 kDa proSP-C. A late processing intermediate, SP-C i, corresponding to residues 12–58 of proSP-C, lacks the surface activity of SP-C, and the SP-Ci a-helical structure does not unfold in contrast to the metastable nature of the SP-C helix. | iFEBS Journal Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C Jing Li1 Edvards Liepinsh1 Andreas Almlen2 Johan Thyberg3 Tore Curstedt2 Hans Jornvall1 and Jan Johansson4 1 Department of MedicalBiochemistry and Biophysics Karolinska Institutet Stockholm Sweden 2 Department of Molecular Medicine and Surgery Karolinska Institutet Stockholm Sweden 3 Department of Celland Molecular Biology Karolinska Institutet Stockholm Sweden 4 Department of Molecular Biosciences Swedish University of AgriculturalSciences The BiomedicalCentre Uppsala Sweden Keywords surfactant protein peptide aggregation proprotein processing peptide structure analysis surface activity Correspondence J. Li Department of MedicalBiochemistry and Biophysics Karolinska Institutet S-17177 Stockholm Sweden Fax 46 8337462 Tel 46 852487681 E-mail Note The coordinates for the NMR structure of SP-Ci 1-31 in DPC micelle have been deposited in the protein data bank under the accession code 2esy. Received 15 November 2005 revised 20 December 2005 accepted 20 December 2005 doi Mature lung surfactant protein C SP-C corresponds to residues 24-58 of the 21 kDa proSP-C. A late processing intermediate SP-Ci corresponding to residues 12-58 of proSP-C lacks the surface activity of SP-C and the SP-Ci a-helical structure does not unfold in contrast to the metastable nature of the SP-C helix. The NMR structure of an analogue of SP-Ci SP-Ci 1-31 with two palmitoylCys replaced by Phe and four Val replaced by Leu in dodecylphosphocholine micelles and in ethanol shows that its a-helix vs. that of SP-C is extended N-terminally. The Arg-Phe part in SP-Ci that is cleaved to generate SP-C is localized in a turn structure which is followed by a short segment in extended conformation. Circular dichroism spectroscopy of SP-Ci 1-31 in microsomal or surfactant lipids shows a mixture of helical and extended conformation at pH

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