1oue
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT
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OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1OUE is a Single protein structure of sequence from Homo sapiens with NA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
The structure, stability, and folding process of amyloidogenic mutant human lysozyme., Funahashi J, Takano K, Ogasahara K, Yamagata Y, Yutani K, J Biochem (Tokyo). 1996 Dec;120(6):1216-23. PMID:9010773
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