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Structures of the rat complement regulator CrrY.
journal contribution
posted on 2019-10-18, 13:01 authored by P Roversi, S Johnson, JJE Caesar, F McLean, KJ Leath, SA Tsiftsoglou, BP Morgan, CL Harris, RB Sim, SM LeaComplement receptor 1-related protein Y (CrrY) is an important cell-surface regulator of complement that is unique to rodent species. The structure of rat CrrY domains 1-4 has been determined in two distinct crystal forms and reveals a 70° bend between domains 3 and 4. Comparisons of this structure with those of other complement regulators suggests that rearrangement of this interface may occur on forming the regulatory complex with C3b.
Funding
PR and SJ were funded by the Wellcome Trust (#083599) and the MRC (#G0400775) Project Grants to SML. The staff at the ESRF ID14-4 and Diamond I04 synchrotron beamlines assisted with data collection. Graeme Winter, Claus Flensburg, Clemens Vonrhein and Oliver Smart helped with data processing and refinement. We are grateful to Ge´rard Bricogne and the members of the Global Phasing Consortium for access to a beta version of the autoBUSTER software.
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Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2011, 67 (Pt 7), pp. 739-743Author affiliation
/Organisation/COLLEGE OF LIFE SCIENCES/School of Medicine/Department of Infection, Immunity and InflammationVersion
- VoR (Version of Record)
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Acta Crystallographica Section F: Structural Biology and Crystallization CommunicationsPublisher
International Union of Crystallographyeissn
1744-3091Acceptance date
2011-05-02Copyright date
2011Available date
2019-10-18Publisher DOI
Publisher version
http://scripts.iucr.org/cgi-bin/paper?S1744309111016551Language
enAdministrator link
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