1lyy

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{{Seed}}
 
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[[Image:1lyy.png|left|200px]]
 
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==AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME==
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The line below this paragraph, containing "STRUCTURE_1lyy", creates the "Structure Box" on the page.
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<StructureSection load='1lyy' size='340' side='right'caption='[[1lyy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1lyy]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LYY FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lyy OCA], [https://pdbe.org/1lyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lyy RCSB], [https://www.ebi.ac.uk/pdbsum/1lyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lyy ProSAT]</span></td></tr>
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{{STRUCTURE_1lyy| PDB=1lyy | SCENE= }}
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8464497</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_HUMAN LYSC_HUMAN] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ly/1lyy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lyy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME===
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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:9039909<ref>PMID:9039909</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1lyy" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9039909}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9039909 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9039909}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1LYY is a 1 chain 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].
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==Reference==
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<ref group="xtra">PMID:9039909</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Blake, C C.F.]]
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[[Category: Blake CCF]]
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[[Category: Sunde, M.]]
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[[Category: Sunde M]]
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[[Category: Beta-1,4-glycan-hydrolase]]
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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 Wed Feb 18 10:12:41 2009''
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Current revision

AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

PDB ID 1lyy

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