1iwy: Difference between revisions
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==Crystal Structure Analysis of Human lysozyme at 170K.== | ==Crystal Structure Analysis of Human lysozyme at 170K.== | ||
<StructureSection load='1iwy' size='340' side='right' caption='[[1iwy]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1iwy' size='340' side='right' caption='[[1iwy]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iwt|1iwt]], [[1iwu|1iwu]], [[1iwv|1iwv]], [[1iww|1iww]], [[1iwx|1iwx]], [[1iwz|1iwz]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iwt|1iwt]], [[1iwu|1iwu]], [[1iwv|1iwv]], [[1iww|1iww]], [[1iwx|1iwx]], [[1iwz|1iwz]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwy OCA], [http://pdbe.org/1iwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwy RCSB], [http://www.ebi.ac.uk/pdbsum/1iwy PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwy OCA], [http://pdbe.org/1iwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iwy RCSB], [http://www.ebi.ac.uk/pdbsum/1iwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iwy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/1iwy_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iw/1iwy_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:46, 17 January 2018
Crystal Structure Analysis of Human lysozyme at 170K.Crystal Structure Analysis of Human lysozyme at 170K.
Structural highlights
Disease[LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM: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.[1] Function[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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe static and dynamic structures of human lysozyme at seven different temperatures ranging from 113 to 178 K were investigated by normal-mode refinement of the cryogenic X-ray diffraction data collected from a single crystal. Normal-mode refinement decomposes the mean-square fluctuations of protein atoms from their average position into the contributions from the internal degrees of freedom, which change the shape of the protein structure, and those from the external degrees of freedom, which generate rigid-body motions in the crystal. While at temperatures below 150 K the temperature dependence of the total mean-square fluctuations shows a small gradient similar to that predicted theoretically by normal-mode analysis, at temperatures above 150 K there is an apparent inflection in the temperature dependence with a higher gradient. The inflection in the temperature dependence at temperatures above 150 K occurs mostly in the external degrees of freedom. Possible causes for the dynamic transition are discussed with respect to the crystal packing and physicochemical properties of crystalline water. Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factors.,Joti Y, Nakasako M, Kidera A, Go N Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1421-32. Epub 2002, Aug 23. PMID:12198298[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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