1lyy

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[[Image:1lyy.jpg|left|200px]]<br /><applet load="1lyy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lyy.jpg|left|200px]]
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caption="1lyy, resolution 1.8&Aring;" />
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'''AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME'''<br />
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{{Structure
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|PDB= 1lyy |SIZE=350|CAPTION= <scene name='initialview01'>1lyy</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]
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|GENE=
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}}
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'''AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LYY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYY OCA].
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1LYY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LYY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9039909 9039909]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9039909 9039909]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:36:47 2008''

Revision as of 10:36, 20 March 2008

Image:1lyy.jpg


PDB ID 1lyy

Drag the structure with the mouse to rotate
, resolution 1.8Å
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME


Contents

Overview

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.

Disease

Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]

About this Structure

1LYY 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

Page seeded by OCA on Thu Mar 20 12:36:47 2008

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