Zobrazeno 1 - 10 of 16 pro vyhledávání: '"B L, Sibanda"'
1
Crystal structure of aspartate decarboxylase at 2.2 Å resolution provides evidence for an ester in protein self–processing
Autor: B. L. Sibanda, Armando Albert, Manoj K. Ramjee, Alison G. Smith, Tom L. Blundell, G. Khan, F. von Delft, Ulrich Genschel, V. Dhanaraj, Michael Witty, R. Pulido, Chris Abell
Publikováno v: Nature Structural Biology. 5:289-293
The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1b70b0378c3e9ace3e04272614a30e7
https://doi.org/10.1038/nsb0498-289
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2
Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin
Autor: B. L. Sibanda, M. Badasso, Jon B. Cooper, Chris Dealwis, S.P. Wood
Publikováno v: Journal of Crystal Growth. 122:393-399
Renin from mouse submandibular glands has been highly purified and co-crystallized with a synthetic nonapeptide fragment of rat angiotensionogen in which the scissile Leu-Leu bond has been modified as a hydroxyethylene mimic of the transition state.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a9cff1bb98b3f77b5bb0f1a9f0a1043c
https://doi.org/10.1016/0022-0248(92)90274-m
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3
X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins
Autor: Steve P. Wood, Kieran F. Geoghegan, Peter M. Hobart, B. L. Sibanda, M. Badasso, C. G. Dealwis, M.P. Newman, B. A. O’Connor, C. Aguilar, Mark Ammirati, Dennis J. Hoover, Ian J. Tickle, Carlos Frazão, V. Dhanaraj, Dennis E. Danley, Tom L. Blundell, Jon B. Cooper, H.P.C. Driessen
Publikováno v: Nature. 357:466-472
X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop reg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b3355ba138c0a02b4c22ffdeda71f5e
https://doi.org/10.1038/357466a0
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4
Crystal structure of an Xrcc4-DNA ligase IV complex
Autor: B L, Sibanda, S E, Critchlow, J, Begun, X Y, Pei, S P, Jackson, T L, Blundell, L, Pellegrini
Publikováno v: Nature structural biology. 8(12)
A complex of two proteins, Xrcc4 and DNA ligase IV, plays a fundamental role in DNA non-homologous end joining (NHEJ), a cellular function required for double-strand break repair and V(D)J recombination. Here we report the crystal structure of human
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d3b96abcfdc79bae2cb265dfe9c559e8
https://pubmed.ncbi.nlm.nih.gov/11702069
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6
Crystallization and preliminary X-ray analysis of complexes of peptide inhibitors with human recombinant and mouse submandibular renins
Autor: Javier Sueiras-Diaz, Tom L. Blundell, Kazuo Murakami, Mark Ammirati, Jon B. Cooper, S.P. Wood, H. Miyazaki, Dennis E. Danley, M. Szelke, D. M. Jones, Peter M. Hobart, B. L. Sibanda, M. Badasso, C. G. Dealwis, Dennis J. Hoover, Carlos Frazão, V. Dhanaraj, A. J. Lanzetti, B. A. O’Connor, Kieran F. Geoghegan
Publikováno v: Journal of molecular biology. 223(2)
Inhibitor-complexed crystals of mouse and human renins suitable for X-ray analysis have been prepared. The mouse renin is complexed with a non-hydrolysable decapeptide analogue of rat angiotensinogen containing a hydroxyethylene isostere in place of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75867b0f74d5914336a459b34a141cc0
https://pubmed.ncbi.nlm.nih.gov/1738157
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9
High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes
Autor: A. Cleasby, Martin J. Valler, Ben M. Dunn, Tom L. Blundell, B. L. Sibanda, Joshua S. Boger, M Szelke, Laurence H. Pearl, Andrew M. Hemmings, S.P. Wood, F.E. Watson, C. G. Norey, S.I. Foundling, Brenda J. Leckie, Jon B. Cooper, John Kay, A Hallett, B. Atrash, D. M. Jone
Publikováno v: Nature. 327:349-352
Inhibitors of the conversion of angiotensinogen to the vasoconstrictor angiotensin II have considerable value as antihypertensive agents. For example, captopril and enalapril are clinically useful as inhibitors of angiotensin-converting enzyme. This
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2873254934020d007ba32ffcb564f059
https://doi.org/10.1038/327349a0
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10
Computer graphics modelling of human renin
Autor: Chirgwin John Mitchell, Jasjit S. Bindra, Beryl W. Dominy, Peter M. Hobart, B. L. Sibanda, Tom L. Blundell, Michael Fogliano
Publikováno v: FEBS Letters. 174:102-111
A model has been constructed using computer graphics for human renin based on the sequence derived from that of the gene and the 3-dimensional structure defined at high resolution for other homologous aspartic proteinases. Human renin can adopt a 3-d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bea27f521be4fe4dfd43c41c5ef12e39
https://doi.org/10.1016/0014-5793(84)81086-8
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