1oud
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | The physicochemical properties of an amyloidogenic mutant human lysozyme | + | The physicochemical properties of an amyloidogenic mutant human lysozyme (Ile56Thr) were examined in order to elucidate the mechanism of amyloid formation. The crystal structure of the mutant protein was the same as the wild-type structure, except that the hydroxyl group of the introduced Thr56 formed a hydrogen bond with a water molecule in the interior of the protein. The other physicochemical properties of the mutant protein in the native state were not different from those of the wild-type protein. However, the equilibrium and kinetic stabilities of the mutant protein were remarkably decreased due to the introduction of a polar residue (Thr) in the interior of the molecule. It can be concluded that the amyloid formation of the mutant human lysozyme is due to a tendency to favor (partly or/and completely) denatured structures. |
==Disease== | ==Disease== | ||
| Line 13: | Line 13: | ||
==Reference== | ==Reference== | ||
| - | The structure, stability, and folding process of amyloidogenic mutant human lysozyme., Funahashi J, Takano K, Ogasahara K, Yamagata Y, Yutani K, J Biochem | + | The structure, stability, and folding process of amyloidogenic mutant human lysozyme., Funahashi J, Takano K, Ogasahara K, Yamagata Y, Yutani K, J Biochem. 1996 Dec;120(6):1216-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9010773 9010773] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
| Line 27: | Line 27: | ||
[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:40 2008'' |
Revision as of 12:21, 21 February 2008
|
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
Contents |
Overview
The physicochemical properties of an amyloidogenic mutant human lysozyme (Ile56Thr) were examined in order to elucidate the mechanism of amyloid formation. The crystal structure of the mutant protein was the same as the wild-type structure, except that the hydroxyl group of the introduced Thr56 formed a hydrogen bond with a water molecule in the interior of the protein. The other physicochemical properties of the mutant protein in the native state were not different from those of the wild-type protein. However, the equilibrium and kinetic stabilities of the mutant protein were remarkably decreased due to the introduction of a polar residue (Thr) in the interior of the molecule. It can be concluded that the amyloid formation of the mutant human lysozyme is due to a tendency to favor (partly or/and completely) denatured structures.
Disease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this Structure
1OUD 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
The structure, stability, and folding process of amyloidogenic mutant human lysozyme., Funahashi J, Takano K, Ogasahara K, Yamagata Y, Yutani K, J Biochem. 1996 Dec;120(6):1216-23. PMID:9010773
Page seeded by OCA on Thu Feb 21 14:21:40 2008
Categories: Homo sapiens | Lysozyme | Single protein | Fujii, S. | Takano, K. | Yamagata, Y. | Yutani, K. | NA | Amyloid | Disease mutation | Hydrolase (o-glycosyl) | Signal
