1wqr

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(New page: 200px<br /> <applet load="1wqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wqr, resolution 1.8&Aring;" /> '''CONTRIBUTION OF HYDR...)
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[[Image:1wqr.gif|left|200px]]<br />
 
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<applet load="1wqr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wqr, resolution 1.8&Aring;" />
 
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'''CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME'''<br />
 
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==Overview==
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==CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME==
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The contribution of hydrogen bonds to the conformational stability of, human lysozyme was investigated by the combination of calorimetric and, X-ray analyses of six Tyr --&gt; Phe mutants. Unfolding Delta G and unfolding, Delta H values of the Tyr --&gt; Phe mutant proteins were changed by from, +0.3 to -4.0 kJ/mol and from 0 to -16 kJ/mol, respectively, compared to, those of the wild-type protein. The net contribution of a hydrogen bond at, a specific site to stability (Delta Gwild/HB), considering factors, affected by substitutions, was evaluated on the basis of X-ray structures, of the mutant proteins. In the present study, one of six mutant proteins, was suitable for evaluating the strength of the hydrogen bond. Delta, Gwild/HB for the intramolecular hydrogen bond at Tyr124 was evaluated to, be 7.5 kJ/mol. Results of the analysis of other mutants also suggest that, hydrogen bonds of the hydroxyl group of Tyr, including the hydrogen bond, with a water molecule, contribute to the stabilization of the human, lysozyme.
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<StructureSection load='1wqr' size='340' side='right'caption='[[1wqr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1wqr]] 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=1WQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WQR FirstGlance]. <br>
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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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1wqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wqr OCA], [https://pdbe.org/1wqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wqr RCSB], [https://www.ebi.ac.uk/pdbsum/1wqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wqr 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/wq/1wqr_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=1wqr ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Amyloidosis, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=153450 153450]], Microphthalmia, syndromic 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=309800 309800]]
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1WQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WQR OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --&gt; phenylalanine mutants., Yamagata Y, Kubota M, Sumikawa Y, Funahashi J, Takano K, Fujii S, Yutani K, Biochemistry. 1998 Jun 30;37(26):9355-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9649316 9649316]
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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: Fujii S]]
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[[Category: Fujii, S.]]
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[[Category: Funahashi J]]
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[[Category: Funahashi, J.]]
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[[Category: Kubota M]]
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[[Category: Kubota, M.]]
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[[Category: Sumikawa Y]]
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[[Category: Sumikawa, Y.]]
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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: CL]]
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[[Category: NA]]
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[[Category: bacteriolytic enzyme]]
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[[Category: glycosidase]]
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[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:53:44 2007''
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Current revision

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

PDB ID 1wqr

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