Structural basis for engagement by complement factor H of C3b on a self surface

Structural basis for engagement by complement factor H of C3b on a self surface

Complement factor H (FH) attenuates C3b molecules tethered via their thioester domains to self-surfaces and thereby protects host tissues. FH is a cofactor for initial C3b proteolysis that ultimately yields a surface-attached fragment (C3d), corresponding to the thioester domain. We used NMR and X-r...

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Bibliographic Details
Main Authors: Morgan, Hugh P., Schmidt, Christoph Q., Guariento, Mara, Blaum, Bärbel S., Gillespie, Dominic, Herbert, Andrew P., Kavanagh, David, Mertens, Haydyn D. T., Svergun, Dmitri I., Johansson, Conny M., Uhrín, Dušan, Barlow, Paul N., Hannan, Jonathan P.
Format: Online
Language:English
Published: 2011
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3512577/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3512577/

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