Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein

Autor: Melina Haupt, Matthew P. Blakeley, Stuart J. Fisher, Sax A. Mason, Jon B. Cooper, Edward P. Mitchell, V. Trevor Forsyth

Publikováno v: IUCrJ, Vol 1, Iss 6, Pp 429-438 (2014)

Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit

Externí odkaz: https://doaj.org/article/1b8281a5213e489194993e77fbdcee08

Preliminary neutron crystallographic study of human transthyretin

Autor: Melina Haupt, Jonathan B. Cooper, V. Trevor Forsyth, Susana C. M. Teixeira, Matthew P. Blakeley, Edward P. Mitchell, Sax A. Mason

Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1428-1431

Preliminary studies of perdeuterated crystals of human transthyretin (TTR) have been carried out using the LADI-III and D19 diffractometers at the Institut Laue-Langevin in Grenoble. The results demonstrate the feasibility of a full crystallographic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58c70404ca248a883767e6cf670238a6
https://doi.org/10.1107/s1744309111036244

Structure of the τ60/Δτ91 Subcomplex of Yeast Transcription Factor IIIC: Insights into Preinitiation Complex Assembly

Autor: Christoph W. Müller, Carlos Fernández-Tornero, Pierre Legrand, Anastasia Mylona, Melina Haupt, Joël Acker, André Sentenac

Publikováno v: Molecular Cell. 24(2):221-232

Yeast RNA polymerase III is recruited upon binding of subcomplexes tauA and tauB of transcription factor IIIC (TFIIIC) to the A and B blocks of tRNA gene promoters. The tauB subcomplex consists of subunits tau60, tau91, and tau138. We determined the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc78f56d0319636ee7bad3e832f4887f

Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein

Autor: Matthew P. Blakeley, Melina Haupt, V.T. Forsyth, Edward P. Mitchell, Jonathan B. Cooper, S. J. Fisher, Sax A. Mason

Publikováno v: 'IUCrJ ', vol: 1, pages: 429-438 (2014)
International Union of Crystallography journal
International Union of Crystallography journal, International Union of Crystallography 2014, 1 (6), pp.429-438. ⟨10.1107/S2052252514021113⟩
IUCrJ
IUCrJ, Vol 1, Iss 6, Pp 429-438 (2014)

A neutron crystallographic study of perdeuterated transthyretin reveals important aspects of the structure relating to its stability and its propensity to form fibrils, as well as evidence of a single water molecule that affects the symmetry of the t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60c9d9d33dba25f8907e78023ace014a

The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone

Autor: Kristina, Irzik, Juliane, Pfrötzschner, Tatjana, Goss, Franziska, Ahnert, Melina, Haupt, Jörg-Christian, Greie

Publikováno v: The FEBS journal. 278(17)

In Bacteria and Archaea, high-affinity potassium uptake is mediated by the ATP-driven KdpFABC complex. On the basis of the biochemical properties of the ATP-hydrolyzing subunit KdpB, the transport complex is classified as type IA P-type ATPase. Howev

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b5e3f465f8006f90d387b4629fa158b2
https://pubmed.ncbi.nlm.nih.gov/21711450