1ouc

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[[Image:1ouc.jpg|left|200px]]<br /><applet load="1ouc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ouc.jpg|left|200px]]
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caption="1ouc, resolution 1.8&Aring;" />
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'''CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT'''<br />
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{{Structure
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|PDB= 1ouc |SIZE=350|CAPTION= <scene name='initialview01'>1ouc</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 110 ([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 V110A MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OUC 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=1OUC OCA].
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1OUC 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=1OUC OCA].
==Reference==
==Reference==
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Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants., Takano K, Yamagata Y, Fujii S, Yutani K, Biochemistry. 1997 Jan 28;36(4):688-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020766 9020766]
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Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants., Takano K, Yamagata Y, Fujii S, Yutani K, Biochemistry. 1997 Jan 28;36(4):688-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9020766 9020766]
[[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 14:21:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:44 2008''

Revision as of 11:15, 20 March 2008

Image:1ouc.jpg


PDB ID 1ouc

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Gene: HUMAN LYSOZYME WITH VAL 110 (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 V110A MUTANT


Contents

Overview

To clarify the contribution of the hydrophobic effect to the conformational stability of human lysozyme, a series of Val to Ala mutants were constructed. The thermodynamic parameters for the denaturation of these nine mutant proteins were determined using differential scanning calorimetry (DSC), and the crystal structures were solved at high resolution. The denaturation Gibbs energy (delta delta G) and enthalpy (delta delta H) values of the mutant proteins ranged from +2.2 to- 6.3 kJ/mol and from +7 to -17 kJ/mol, respectively. The structural analyses showed that the mutation site and/or the residues around it in some proteins shifted toward the created cavity, and the substitutions affected not only the mutations site but also other parts far from the site, although the structural changes were not as great. Correlation between the changes in the thermodynamic parameters and the structural features of mutant proteins was examined, including the five Ile to Val mutant human lysozymes [Takano et al. (1995) J. Mol. Biol. 254, 62-76]. There was no simple general correlation between delta delta G and the changes in hydrophobic surface area exposed upon denaturation (delta delta ASAHP). We found only a new correlation between the delta delta G and delta delta ASAHP of all of the hydrophobic residues if the effect of the secondary structure propensity was taken into account.

Disease

Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]

About this Structure

1OUC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants., Takano K, Yamagata Y, Fujii S, Yutani K, Biochemistry. 1997 Jan 28;36(4):688-98. PMID:9020766

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