1c46

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[[Image:1c46.jpg|left|200px]]<br /><applet load="1c46" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1c46.jpg|left|200px]]
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caption="1c46, resolution 2.2&Aring;" />
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'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''<br />
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{{Structure
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|PDB= 1c46 |SIZE=350|CAPTION= <scene name='initialview01'>1c46</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND=
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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=
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}}
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'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1C46 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1C46 OCA].
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1C46 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=1C46 OCA].
==Reference==
==Reference==
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Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10561612 10561612]
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Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10561612 10561612]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: stability]]
[[Category: stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:02:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:34 2008''

Revision as of 08:19, 20 March 2008


PDB ID 1c46

Drag the structure with the mouse to rotate
, resolution 2.2Å
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES


Contents

Overview

To minutely understand the effect of foreign N-terminal residues on the conformational stability of human lysozyme, five mutant proteins were constructed: two had Met or Ala in place of the N-terminal Lys residue (K1M and K1A, respectively), and others had one additional residue, Met, Gly or Pro, to the N-terminal Lys residue (Met(-1), Gly(-1) and Pro(-1), respectively). The thermodynamic parameters for denaturation of these mutant proteins were examined by differential scanning calorimetry and were compared with that of the wild-type protein. Three mutants with the extra residue were significantly destabilized: the changes in unfolding Gibbs energy (DeltaDeltaG) were -9.1 to -12.2 kJ.mol-1. However, the stability of two single substitutions at the N-terminal slightly decreased; the DeltaDeltaG values were only -0.5 to -2.5 kJ.mol-1. The results indicate that human lysozyme is destabilized by an expanded N-terminal residue. The crystal structural analyses of K1M, K1A and Gly(-1) revealed that the introduction of a residue at the N-terminal of human lysozyme caused the destruction of hydrogen bond networks with ordered water molecules, resulting in the destabilization of the protein.

Disease

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

About this Structure

1C46 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:10561612

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