1ioc
From Proteopedia
(New page: 200px<br /> <applet load="1ioc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ioc, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1ioc.gif|left|200px]]<br /> | + | [[Image:1ioc.gif|left|200px]]<br /><applet load="1ioc" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1ioc, resolution 2.4Å" /> | caption="1ioc, resolution 2.4Å" /> | ||
'''CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T'''<br /> | '''CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T'''<br /> | ||
==Overview== | ==Overview== | ||
| - | To understand the mechanism of amyloid fibril formation of a protein, we | + | 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 > EAEA > I56T > wild-type. This order is almost the reverse of the order of conformational stability of these proteins, wild-type > EAEA > I56T > 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=NA:'>NA</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOC OCA]. |
==Reference== | ==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 | + | 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. 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: Lysozyme]] | ||
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[[Category: stability]] | [[Category: stability]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:53 2008'' |
Revision as of 11:13, 21 February 2008
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CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T
Contents |
Overview
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 > EAEA > I56T > wild-type. This order is almost the reverse of the order of conformational stability of these proteins, wild-type > EAEA > I56T > 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.
Disease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this Structure
1IOC is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
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. 2002 Oct;132(4):655-61. PMID:12359083
Page seeded by OCA on Thu Feb 21 13:13:53 2008
Categories: Homo sapiens | Lysozyme | Single protein | Goda, S. | Takano, K. | Yamagata, Y. | Yutani, K. | NA | Amyloid | Human lysozyme | Mutant | Stability
