1ckg: Difference between revisions

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{{Seed}}
[[Image:1ckg.png|left|200px]]


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==T52V MUTANT HUMAN LYSOZYME==
The line below this paragraph, containing "STRUCTURE_1ckg", creates the "Structure Box" on the page.
<StructureSection load='1ckg' size='340' side='right'caption='[[1ckg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ckg]] is a 2 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=1CKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CKG FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#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=1ckg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ckg OCA], [https://pdbe.org/1ckg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ckg RCSB], [https://www.ebi.ac.uk/pdbsum/1ckg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ckg ProSAT]</span></td></tr>
{{STRUCTURE_1ckg| PDB=1ckg |  SCENE= }}
</table>
== Disease ==
[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>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/1ckg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1ckg ConSurf].
<div style="clear:both"></div>


===T52V MUTANT HUMAN LYSOZYME===
==See Also==
 
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_10504240}}
 
==About this Structure==
1CKG 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=1CKG OCA].
 
==Reference==
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,)., Takano K, Yamagata Y, Funahashi J, Hioki Y, Kuramitsu S, Yutani K, Biochemistry. 1999 Sep 28;38(39):12698-708. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10504240 10504240]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Funahashi J]]
[[Category: Funahashi, J.]]
[[Category: Takano K]]
[[Category: Takano, K.]]
[[Category: Yamagata Y]]
[[Category: Yamagata, Y.]]
[[Category: Yutani K]]
[[Category: Yutani, K.]]
[[Category: Hydrogen bond]]
[[Category: Stability]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:07 2008''

Latest revision as of 08:57, 3 April 2024

T52V MUTANT HUMAN LYSOZYMET52V MUTANT HUMAN LYSOZYME

Structural highlights

1ckg is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al.. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993 Apr 8;362(6420):553-7. PMID:8464497 doi:http://dx.doi.org/10.1038/362553a0

1ckg, resolution 2.20Å

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