1loz

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{{STRUCTURE_1loz| PDB=1loz | SCENE= }}
{{STRUCTURE_1loz| PDB=1loz | SCENE= }}
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'''AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME'''
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===AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME===
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==Overview==
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Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
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{{ABSTRACT_PUBMED_9039909}}
==About this Structure==
==About this Structure==
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[[Category: Enzyme]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:08:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:40:24 2008''

Revision as of 18:40, 2 July 2008

Image:1loz.png

Template:STRUCTURE 1loz

AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME

Template:ABSTRACT PUBMED 9039909

About this Structure

1LOZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis., Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CC, Pepys MB, Nature. 1997 Feb 27;385(6619):787-93. PMID:9039909

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