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PDBsum entry 1ioc
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Elongation in a beta-Structure promotes amyloid-Like fibril formation of human lysozyme.
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Authors
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S.Goda,
K.Takano,
Y.Yamagata,
S.Maki,
K.Namba,
K.Yutani.
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Ref.
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J Biochem (tokyo), 2002,
132,
655-661.
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PubMed id
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Abstract
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To understand the mechanism of amyloid fibril formation of a protein, we
examined wild-type and three mutant human lysozymes containing both
amyloidogenic and non-amyloidogenic proteins: I56T (amyloidogenic); EAEA, which
has four additional residues (Glu-Ala-Glu-Ala-) at the N-terminus located on a
beta-structure; and EAEA-I56T, which is an I56T mutant of EAEA. All formed
amyloid-like fibrils through an in the increase contents of alpha-helix with
increasing concentration of ethanol. The order of propensity for amyloid-like
fibril formation in highly concentrated ethanol solution is EAEA-I56T > EAEA
> I56T > wild-type. This order is almost the reverse of the order of
conformational stability of these proteins, wild-type > EAEA > I56T >
EAEA-I56T. The important views in this work are as follows. (i) Artificially
modified proteins formed amyloid fibrils in vitro. This means that amyloid
formation is a generic property of polypeptide chains. (ii) The amyloidogenic
mutation Ile56 to Thr caused the destabilization and promoted fibril formation
in the wild-type and EAEA human lysozymes, indicating that instability
facilitates amyloid formation. (iii) The mutant protein EAEA human lysozyme had
higher propensity for fibril formation than the amyloidogenic mutant protein,
indicating that amyloid formation is controlled not only by stability but also
by other factors. In this case, appending polypeptide chains to a beta-structure
accelerated amyloid formation.
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Secondary reference #1
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Title
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Effect of extra n-Terminal residues on the stability and folding of human lysozyme expressed in pichia pastoris.
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Authors
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S.Goda,
K.Takano,
Y.Yamagata,
Y.Katakura,
K.Yutani.
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Ref.
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Protein Eng, 2000,
13,
299-307.
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PubMed id
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