1oud

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[[Image:1oud.jpg|left|200px]]<br /><applet load="1oud" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oud.jpg|left|200px]]
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caption="1oud, resolution 1.8&Aring;" />
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'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT'''<br />
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{{Structure
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|PDB= 1oud |SIZE=350|CAPTION= <scene name='initialview01'>1oud</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|ACTIVITY= [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]
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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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}}
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'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OUD 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=1OUD OCA].
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1OUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUD OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/9010773 9010773]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: signal]]
[[Category: signal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:42 2008''

Revision as of 11:15, 20 March 2008

Image:1oud.jpg


PDB ID 1oud

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Gene: HUMAN LYSOZYME WITH VAL 121 (Homo sapiens)
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 13:15:42 2008

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