1lhi

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{{Seed}}
 
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[[Image:1lhi.png|left|200px]]
 
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==ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS==
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The line below this paragraph, containing "STRUCTURE_1lhi", creates the "Structure Box" on the page.
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<StructureSection load='1lhi' size='340' side='right'caption='[[1lhi]], [[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'>[[1lhi]] 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=1LHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LHI 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=1lhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lhi OCA], [https://pdbe.org/1lhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lhi RCSB], [https://www.ebi.ac.uk/pdbsum/1lhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lhi ProSAT]</span></td></tr>
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{{STRUCTURE_1lhi| PDB=1lhi | 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/lh/1lhi_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=1lhi ConSurf].
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<div style="clear:both"></div>
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===ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS===
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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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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 1643041 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_1643041}}
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==About this Structure==
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1LHI 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=1LHI OCA].
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==Reference==
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Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants., Herning T, Yutani K, Inaka K, Kuroki R, Matsushima M, Kikuchi M, Biochemistry. 1992 Aug 11;31(31):7077-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1643041 1643041]
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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: Herning T]]
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[[Category: Herning, T.]]
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[[Category: Inaka K]]
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[[Category: Inaka, K.]]
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[[Category: Kikuchi M]]
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[[Category: Kikuchi, M.]]
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[[Category: Kuroki R]]
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[[Category: Kuroki, R.]]
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[[Category: Matsushima M]]
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[[Category: Matsushima, M.]]
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[[Category: Yutani K]]
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[[Category: Yutani, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:55:14 2008''
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Current revision

ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS

PDB ID 1lhi

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