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PDBsum entry 5cnh
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Transport protein
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PDB id
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5cnh
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PDB id:
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| Name: |
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Transport protein
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Title:
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X-ray structure of perdeuterated wild-type ttr at 1.42a resolution
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Structure:
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Transthyretin. Chain: a, b. Fragment: unp residues 21-147. Synonym: attr,prealbumin,tbpa. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ttr, palb. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.42Å
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R-factor:
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0.154
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R-free:
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0.198
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Authors:
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A.W.Yee,M.Moulin,E.Mossou,M.Haertlein,E.P.Mitchell,J.B.Cooper, V.T.Forsyth
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Key ref:
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A.W.Yee
et al.
(2016).
Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses.
Angew Chem Int Ed Engl,
55,
9292-9296.
PubMed id:
DOI:
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Date:
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17-Jul-15
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Release date:
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06-Jul-16
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PROCHECK
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Headers
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References
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P02766
(TTHY_HUMAN) -
Transthyretin from Homo sapiens
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Seq:
Struc:
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147 a.a.
116 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Angew Chem Int Ed Engl
55:9292-9296
(2016)
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PubMed id:
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Impact of Deuteration on the Assembly Kinetics of Transthyretin Monitored by Native Mass Spectrometry and Implications for Amyloidoses.
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A.W.Yee,
M.Moulin,
N.Breteau,
M.Haertlein,
E.P.Mitchell,
J.B.Cooper,
E.Boeri Erba,
V.T.Forsyth.
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ABSTRACT
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It is well established that the formation of transthyretin (TTR) amyloid fibrils
is linked to the destabilization and dissociation of its tetrameric structure
into insoluble aggregates. Isotope labeling is used for the study of TTR by NMR,
neutron diffraction, and mass spectrometry (MS). Here MS, thioflavin T
fluorescence, and crystallographic data demonstrate that while the X-ray
structures of unlabeled and deuterium-labeled TTR are essentially identical,
subunit exchange kinetics and amyloid formation are accelerated for the
deuterated protein. However, a slower subunit exchange is noted in deuterated
solvent, reflecting the poorer solubility of non-polar protein side chains in
such an environment. These observations are important for the interpretation of
kinetic studies involving deuteration. The destabilizing effects of TTR
deuteration are rather similar in character to those observed for aggressive
mutations of TTR such as L55P (associated with familial amyloid polyneuropathy).
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Links
