Affiliation: University of Leicester
- Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponinJanice Bramham
Department of Biochemistry, University of Leicester, Adrian Building, University Road, Leicester LE1 7RH, United Kingdom
Structure 10:249-58. 2002..We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins...
- Structural diversity in p160/CREB-binding protein coactivator complexesLorna Waters
Department of Biochemistry, Henry Wellcome Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, United Kingdom
J Biol Chem 281:14787-95. 2006....
- Functional insights from the structure of the multifunctional C345C domain of C5 of complementJanice Bramham
Schools of Chemistry and Biological Sciences, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, Scotland, UK
J Biol Chem 280:10636-45. 2005..Modeling of homologous domains from complement proteins C3 and C4, which do not participate in membrane attack complex assembly, suggests that this provisionally identified C6/C7-interacting face is indeed specific to C5...
- 1H, 15N and 13C resonance assignments of the C345C domain of the complement component C5Janice Bramham
J Biomol NMR 29:217-8. 2004
- ZZ domain of dystrophin and utrophin: topology and mapping of a beta-dystroglycan interaction siteKarim Hnia
Universite Montpellier 1, Unité de Formation et de Recherche de Médecine, Laboratoire de Physiologie des Interactions, Institut de Biologie, Boulevard Henri IV, F 34062, France
Biochem J 401:667-77. 2007..Our results suggest that residues 3326-3332 of dystrophin form a crucial part of the contact region between dystrophin and beta-dystroglycan and provide new insight into ZZ domain organization and function...