Journal of Molecular Biology
Volume 424, Issue 5, 14 December 2012, Pages 295-312
Solution Structure of CCP Modules 10–12 Illuminates Functional Architecture of the Complement Regulator, Factor H
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Graphical abstract
Highlights
► The 20-CCP‐module human protein FH prevents complement-mediated tissue damage. ► NMR structures of CCPs 10–11 and 11–12 suggest that this region enhances flexional strength of FH. ► Concatenating bi-modules helps interpret small‐angle X‐ray scattering data, revealing highly compacted arrangement of CCPs 13, 14 and 15. ► Apparent structural dependency of CCP 14 on neighbors could provide a switch between ordered and flexible FH architectures.
Abbreviations
CCP
complement control protein
CR1
complement receptor type 1
DAF
decay accelerating factor
FH
factor H
EOM
ensemble optimization method
HSQC
heteronuclear single quantum coherence
MCP
membrane cofactor protein
NOE
nuclear Overhauser enhancement
SAXS
small-angle X-ray scattering
TOCSY
total correlated spectroscopy
Keywords
protein NMR
protein domains
complement system
small-angle X-ray scattering
regulators of complement activation
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Present addresses: H. D. T. Mertens, Australian Synchrotron, 800 Blackburn Road, Clayton VIC 3168, Australia; C. Q. Schmidt, Institute of Pharmacology of Natural Products and Clinical Pharmacology, Ulm University, Helmholtzstrasse 20, D-89081 Ulm, Germany.
Copyright © 2012 Elsevier Ltd. Published by Elsevier Ltd.