The Regulatory SCR-1/5 and Cell Surface-binding SCR-16/20 Fragments of Factor H Reveal Partially Folded-back Solution Structures and Different Self-associative Properties
- 4 January 2008
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 375 (1), 80-101
- https://doi.org/10.1016/j.jmb.2007.09.026
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndromeThe EMBO Journal, 2006
- The C-terminus of complement regulator Factor H mediates target recognition: evidence for a compact conformation of the native proteinClinical and Experimental Immunology, 2006
- An interactive web database of factor H-associated hemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutationsHuman Mutation, 2005
- Complement Factor H Polymorphism in Age-Related Macular DegenerationScience, 2005
- Solution Structure of the Complex between CR2 SCR 1-2 and C3d of Human Complement: An X-ray Scattering and Sedimentation Modelling StudyJournal of Molecular Biology, 2005
- Solution Structure of Human and Bovine β2-Glycoprotein I Revealed by Small-angle X-ray ScatteringJournal of Molecular Biology, 2002
- Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation ModelingBiophysical Journal, 2000
- The fab and fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling 1 1Edited by R. HuberJournal of Molecular Biology, 1999
- Solution Structure of a Pair of Complement Modules by Nuclear Magnetic ResonanceJournal of Molecular Biology, 1993
- Low-resolution structural studies of mitochondrial ubiquinol: Cytochrome c reductase in detergent solutions by neutron scatteringJournal of Molecular Biology, 1983