1oud: Difference between revisions

Revision as of 04:17, 3 May 2008

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT

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.

About this StructureAbout this Structure

1OUD is a Single protein structure of sequence from Homo sapiens. 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. 1996 Dec;120(6):1216-23. PMID:9010773 Page seeded by OCA on Sat May 3 04:17:31 2008

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OCA

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 [[Image:1oud.jpg|left|200px]]
- {{Structure
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-|ACTIVITY= <span class='plainlinks'>[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] </span>
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-|GENE= HUMAN LYSOZYME WITH VAL 121 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+-->
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-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oud OCA], [http://www.ebi.ac.uk/pdbsum/1oud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oud RCSB]</span>
-}}
 '''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT'''
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 [[Category: Yamagata, Y.]]
 [[Category: Yutani, K.]]
-[[Category: amyloid]]
+[[Category: Amyloid]]
-[[Category: disease mutation]]
+[[Category: Disease mutation]]
-[[Category: hydrolase (o-glycosyl)]]
+[[Category: Signal]]
-[[Category: signal]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:17:31 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:29 2008''