This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ioc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ioc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ioc, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Current revision (06:02, 3 April 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ioc.gif|left|200px]]<br />
 
-
<applet load="1ioc" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ioc, resolution 2.4&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T==
-
To understand the mechanism of amyloid fibril formation of a protein, we, examined wild-type and three mutant human lysozymes containing both, amyloidogenic and non-amyloidogenic proteins: I56T (amyloidogenic); EAEA, which has four additional residues (Glu-Ala-Glu-Ala-) at the N-terminus, located on a beta-structure; and EAEA-I56T, which is an I56T mutant of, EAEA. All formed amyloid-like fibrils through an in the increase contents, of alpha-helix with increasing concentration of ethanol. The order of, propensity for amyloid-like fibril formation in highly concentrated, ethanol solution is EAEA-I56T &gt; EAEA &gt; I56T &gt; wild-type. This order is, almost the reverse of the order of conformational stability of these, proteins, wild-type &gt; EAEA &gt; I56T &gt; EAEA-I56T. The important views in this, work are as follows. (i) Artificially modified proteins formed amyloid, fibrils in vitro. This means that amyloid formation is a generic property, of polypeptide chains. (ii) The amyloidogenic mutation Ile56 to Thr caused, the destabilization and promoted fibril formation in the wild-type and, EAEA human lysozymes, indicating that instability facilitates amyloid, formation. (iii) The mutant protein EAEA human lysozyme had higher, propensity for fibril formation than the amyloidogenic mutant protein, indicating that amyloid formation is controlled not only by stability but, also by other factors. In this case, appending polypeptide chains to a, beta-structure accelerated amyloid formation.
+
<StructureSection load='1ioc' size='340' side='right'caption='[[1ioc]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ioc]] 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=1IOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOC FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
 +
<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>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ioc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioc OCA], [https://pdbe.org/1ioc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ioc RCSB], [https://www.ebi.ac.uk/pdbsum/1ioc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ioc ProSAT]</span></td></tr>
 +
</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/io/1ioc_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=1ioc ConSurf].
 +
<div style="clear:both"></div>
-
==Disease==
+
==See Also==
-
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]]
+
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1IOC 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 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1IOC OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme., Goda S, Takano K, Yamagata Y, Maki S, Namba K, Yutani K, J Biochem (Tokyo). 2002 Oct;132(4):655-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12359083 12359083]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Lysozyme]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Goda S]]
-
[[Category: Goda, S.]]
+
[[Category: Takano K]]
-
[[Category: Takano, K.]]
+
[[Category: Yamagata Y]]
-
[[Category: Yamagata, Y.]]
+
[[Category: Yutani K]]
-
[[Category: Yutani, K.]]
+
-
[[Category: NA]]
+
-
[[Category: amyloid]]
+
-
[[Category: human lysozyme]]
+
-
[[Category: mutant]]
+
-
[[Category: stability]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:32:23 2007''
+

Current revision

CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T

PDB ID 1ioc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ioc"
Personal tools