Genomes and Genes
N H Keep
Affiliation: University of London
- The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophinN H Keep
MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK
J Mol Biol 285:1257-64. 1999..Here, we present the 2.0 A structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin...
- Bacterial resuscitation factors: revival of viable but non-culturable bacteriaN H Keep
School of Crystallography and Institute of Structural Molecular Biology, Birkbeck, University of London, Malet Street, London, WC1E 7HX, United Kingdom
Cell Mol Life Sci 63:2555-9. 2006
- Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimerN H Keep
MRC Laboratory of Molecular Biology, Cambridge, UK
Structure 7:1539-46. 1999..Utrophin is the autosomal homologue of dystrophin, the protein defective in the X-linked Duchenne and Becker muscular dystrophies, and upregulation of utrophin has been suggested as a potential therapy for muscular dystrophy patients...
- The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophyF L Norwood
Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, CB2 2QH, UK
Structure 8:481-91. 2000..Pathogenic mutations in dystrophin result in Duchenne or Becker muscular dystrophy...
- The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activationS D Edwards
BBSRC Bloomsbury Centre for Structural Biology and School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK
Biochemistry 40:7061-8. 2001..More interestingly, a negatively charged peptide binds to the inositol site in a crystal contact and causes a greater conformational change in the structure than inositol...
- Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20C Bagneris
Department of Crystallography, Birkbeck College, Institute of Structural and Molecular Biology, Malet Street, London WC1E 7HX, UK
J Mol Biol 392:1242-52. 2009..The empty pockets and groove provide a starting model for designing drugs to inhibit those sHsps that have a negative effect on cancer treatment...
- Crystal structure of R120G disease mutant of human αB-crystallin domain dimer shows closure of a grooveA R Clark
Department of Biological Sciences, Crystallography, Institute of Structural and Molecular Biology, Birkbeck College, Malet Street, London WC1E 7HX, UK
J Mol Biol 408:118-34. 2011..We speculate that the αB R120G mutation disturbs oligomer dynamics, causing the growth of large soluble oligomers that are toxic to cells by blocking essential processes...
- A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal armN H Keep
Department of Medicine, University College London, Rayne Institute, 5 University Street, London, WC1E 6JJ, UK
Structure 5:623-33. 1997..Guanine nucleotide dissociation inhibitors (GDIs) of the rhoGDI family bind to these G proteins and regulate their activity by preventing nucleotide dissociation and by controlling their interaction with membranes...
- Mapping the binding site for the GTP-binding protein Rac-1 on its inhibitor RhoGDI-1L Y Lian
Department of Biochemistry and Biological NMR Centre, University of Leicester, Leicester, LE1 7RH, UK
Structure 8:47-55. 2000..The cytosolic guanine nucleotide dissociation inhibitors, RhoGDIs, regulate both the GDP/GTP exchange cycle and the membrane association/dissociation cycle...
- Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABA(A) receptor associated protein (GABARAP)R Harris
J Biomol NMR 21:185-6. 2001