critical structural and functional roles for the n-terminal insertion sequence in surfactant protein b analogs关键的氨基端插入序列的结构和功能角色表面活性剂蛋白b类似物.pdfVIP

Critical Structural and Functional Roles for the N-Terminal Insertion Sequence in Surfactant Protein B Analogs 1,2 1,3 1 1 4 Frans J. Walther *, Alan J. Waring , Jose M. Hernandez-Juviel , Larry M. Gordon , Zhengdong Wang , 3 3 5 5 5 Chun-Ling Jung , Piotr Ruchala , Andrew P. Clark , Wesley M. Smith , Shantanu Sharma , Robert H. Notter4,6 1 Los Angeles Biomedical Research Institute at Harbor, University of California Los Angeles Medical Center, Torrance, California, United States of America, 2 Department of Pediatrics, Leiden University Medical Center, Leiden, The Netherlands, 3 Department of Medicine, University of California Los Angeles, Los Angeles, California, United States of America, 4 Department of Pediatrics, University of Rochester, Rochester, New York, United States of America, 5 Department of Chemistry and Center for Macromolecular Modeling and Materials Design, California State Polytechnic University, Pomona, California, United States of America, 6 Department of Environmental Medicine, University of Rochester, Rochester, New York, United States of America Abstract Background: Surfactant protein B (SP-B; 79 residues) belongs to the saposin protein superfamily, and plays functional roles in lung surfactant. The disulfide cross-linked, N- and C-terminal domains of SP-B have been theoretically predicted to fold as charged, amphipathic helices, suggesting their participation in surfactant activities. Earlier structural studies with Mini-B, a disulfide-linked construct based on the N- and C-terminal regions of SP-B (i.e., ,residues 8–25 and 63–78), confirmed that these nei