Domain structure of human complement C4b extends with increasing NaCl concentration: implications for its regulatory mechanism
作者： Ka Wai Fung , David W. Wright , Jayesh Gor , Marcus J. Swann , Stephen J. Perkins
DOI: 10.1042/BCJ20160744
关键词: Scattering 、 Crystallography 、 Thioester 、 Monomer 、 Activator (genetics) 、 Complement C4b 、 Sedimentation coefficient 、 Macroglobulin 、 Chemistry 、 Crystal structure
摘要: During the activation of complement C4 to C4b, exposure its thioester domain (TED) is crucial for attachment C4b activator surfaces. In crystal structure, TED forms an Arg 104 -Glu 1032 salt bridge tether neighbouring macroglobulin (MG1) domain. Here, we examined structure test whether this affects conformation. Dual polarisation interferometry immobilised at a sensor surface showed that maximum thickness increased by 0.46 nm with increase in NaCl concentration from 50 mM 175 NaCl. Analytical ultracentrifugation sedimentation coefficient s 20, w monomeric 8.41 S buffer decreased 7.98 137 buffer, indicating became more extended. Small angle X-ray scattering reported similar R G values 4.89-4.90 137-250 Atomistic modelling conformation and MG1 were separated 4.7 NaCl, being greater than 4.0 structure. Our data reveal low concentrations, both surfaces solution, compact TED-MG1 structures. physiologically-relevant concentrations lead separation domain, making less able bind regulators. These conformational changes are those seen previously C3b, confirming importance regulating C3b.
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biochemj.org参考文章(50)
Andrew Alan Reeves, Theoretical studies of one-dimensional and two-dimensional photonic structures Durham University. ,(2004)
Alister W. Dodds, Small-scale preparation of complement components C3 and C4. Methods in Enzymology. ,vol. 223, pp. 46- 61 ,(1993) , 10.1016/0076-6879(93)23037-N
Stephen J. PERKINS, Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. FEBS Journal. ,vol. 157, pp. 169- 180 ,(1986) , 10.1111/J.1432-1033.1986.TB09653.X
Y. Yang, E.K. Chung, B. Zhou, K. Lhotta, L.A. Hebert, D.J. Birmingham, B.H. Rovin, Y. Yu, The intricate role of complement component C4 in human systemic lupus erythematosus. Current directions in autoimmunity. ,vol. 7, pp. 98- 132 ,(2004) , 10.1159/000075689
John Atkinson, A. C. Chan, Oligosaccharide structure of human C4. Journal of Immunology. ,vol. 134, pp. 1790- 1798 ,(1985)
Maria L. Barilla-LaBarca, M. Kathryn Liszewski, John D. Lambris, Dennis Hourcade, John P. Atkinson, Role of membrane cofactor protein (CD46) in regulation of C4b and C3b deposited on cells Journal of Immunology. ,vol. 168, pp. 6298- 6304 ,(2002) , 10.4049/JIMMUNOL.168.12.6298
Stephen J. Perkins, Azubuike I. Okemefuna, Anira N. Fernando, Alexandra Bonner, Hannah E. Gilbert, Patricia B. Furtado, X-Ray and Neutron Scattering Data and Their Constrained Molecular Modeling Methods in Cell Biology. ,vol. 84, pp. 375- 423 ,(2008) , 10.1016/S0091-679X(07)84013-1
Sofia Mortensen, Rune T Kidmose, Steen V Petersen, Ágnes Szilágyi, Zoltan Prohászka, Gregers R Andersen, None, Structural Basis for the Function of Complement Component C4 within the Classical and Lectin Pathways of Complement Journal of Immunology. ,vol. 194, pp. 5488- 5496 ,(2015) , 10.4049/JIMMUNOL.1500087
T Seya, H Kitamura, M Matsumoto, R P Levine, T Masaki, R Yasuda, A covalent dimer of complement C4b serves as a subunit of a novel C5 convertase that involves no C3 derivatives. Journal of Immunology. ,vol. 147, pp. 927- 932 ,(1991)
Huaying Zhao, Rodolfo Ghirlando, Carlos Alfonso, Fumio Arisaka, Ilan Attali, David L Bain, Marina M Bakhtina, Donald F Becker, Gregory J Bedwell, Ahmet Bekdemir, Tabot MD Besong, Catherine Birck, Chad A Brautigam, William Brennerman, Olwyn Byron, Agnieszka Bzowska, Jonathan B Chaires, Catherine T Chaton, Helmut Cölfen, Keith D Connaghan, Kimberly A Crowley, Ute Curth, Tina Daviter, William L Dean, Ana I Díez, Christine Ebel, Debra M Eckert, Leslie E Eisele, Edward Eisenstein, Patrick England, Carlos Escalante, Jeffrey A Fagan, Robert Fairman, Ron M Finn, Wolfgang Fischle, José García De La Torre, Jayesh Gor, Henning Gustafsson, Damien Hall, Stephen E Harding, José G Hernández Cifre, Andrew B Herr, Elizabeth E Howell, Richard S Isaac, Shu-Chuan Jao, Davis Jose, Soon-Jong Kim, Bashkim Kokona, Jack A Kornblatt, Dalibor Kosek, Elena Krayukhina, Daniel Krzizike, Eric A Kusznir, Hyewon Kwon, Adam Larson, Thomas M Laue, Aline Le Roy, Andrew P Leech, Hauke Lilie, Karolin Luger, Juan R Luque-Ortega, Jia Ma, Carrie A May, Ernest L Maynard, Anna Modrak-Wojcik, Yee-Foong Mok, Norbert Mücke, Luitgard Nagel-Steger, Geeta J Narlikar, Masanori Noda, Amanda Nourse, Tomas Obsil, Chad K Park, Jin-Ku Park, Peter D Pawelek, Erby E Perdue, Stephen J Perkins, Matthew A Perugini, Craig L Peterson, Martin G Peverelli, Grzegorz Piszczek, Gali Prag, Peter E Prevelige, Bertrand DE Raynal, Lenka Rezabkova, Klaus Richter, Alison E Ringel, Rose Rosenberg, Arthur J Rowe, Arne C Rufer, David J Scott, Javier G Seravalli, Alexandra S Solovyova, Renjie Song, David Staunton, Caitlin Stoddard, Katherine Stott, Holger M Strauss, Werner W Streicher, John P Sumida, Sarah G Swygert, Roman H Szczepanowski, Ingrid Tessmer, Ronald T Toth IV, Ashutosh Tripathy, Susumu Uchiyama, Stephan FW Uebel, Satoru Unzai, Anna Vitlin Gruber, Peter H Von Hippel, Christine Wandrey, Szu-Huan Wang, Steven E Weitzel, Beata Wielgus-Kutrowska, Cynthia Wolberger, Martin Wolff, Edward Wright, Yu-Sung Wu, Jacinta M Wubben, Peter Schuck, None, A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation PLOS ONE. ,vol. 10, pp. e0126420- ,(2015) , 10.1371/JOURNAL.PONE.0126420