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International Union of Crystallography, Acta Crystallographica Section D: Biological Crystallography, 3(70), p. 733-743

DOI: 10.1107/s1399004713032549

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Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D

Journal article published in 2014 by Federico Forneris ORCID, B. Tom Burnley, B. Tom Burnley, Piet Gros ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Ensemble-refinement analysis of native and mutant factor D (FD) crystal structures indicates a dynamical transition in FD from a self-inhibited inactive conformation to a substrate-bound active conformation that is reminiscent of the allostery in thrombin. Comparison with previously observed dynamics in thrombin using NMR data supports the crystallographic ensembles.