2mef

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{{Seed}}
 
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[[Image:2mef.png|left|200px]]
 
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==CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME==
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The line below this paragraph, containing "STRUCTURE_2mef", creates the "Structure Box" on the page.
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<StructureSection load='2mef' size='340' side='right'caption='[[2mef]], [[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'>[[2mef]] 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=2MEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MEF 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_2mef| PDB=2mef | SCENE= }}
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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=2mef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mef OCA], [https://pdbe.org/2mef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mef RCSB], [https://www.ebi.ac.uk/pdbsum/2mef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mef ProSAT]</span></td></tr>
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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/me/2mef_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2mef ConSurf].
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<div style="clear:both"></div>
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===CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME===
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_10556244}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 10556244 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_10556244}}
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==About this Structure==
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2MEF 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=2MEF OCA].
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==Reference==
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Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme., Funahashi J, Takano K, Yamagata Y, Yutani K, Protein Eng. 1999 Oct;12(10):841-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10556244 10556244]
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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: Single protein]]
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[[Category: Funahashi J]]
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[[Category: Funahashi, J.]]
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[[Category: Takano K]]
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[[Category: Takano, K.]]
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[[Category: Yamagata Y]]
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[[Category: Yamagata, Y.]]
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[[Category: Yutani K]]
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[[Category: Yutani, K.]]
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[[Category: Alpha + beta]]
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[[Category: Enzyme]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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[[Category: O-glycosyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:50:56 2008''
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Current revision

CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

PDB ID 2mef

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