2hec

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[[Image:2hec.jpg|left|200px]]<br /><applet load="2hec" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hec.jpg|left|200px]]
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caption="2hec, resolution 1.8&Aring;" />
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'''CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''<br />
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{{Structure
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|PDB= 2hec |SIZE=350|CAPTION= <scene name='initialview01'>2hec</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 ILE 56 REP ([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 WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2HEC 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=2HEC OCA].
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2HEC 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=2HEC OCA].
==Reference==
==Reference==
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Contribution of water molecules in the interior of a protein to the conformational stability., Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K, J Mol Biol. 1997 Nov 21;274(1):132-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9398521 9398521]
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Contribution of water molecules in the interior of a protein to the conformational stability., Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K, J Mol Biol. 1997 Nov 21;274(1):132-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9398521 9398521]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
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[[Category: o-glycosyl]]
[[Category: o-glycosyl]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:15:56 2008''

Revision as of 15:15, 20 March 2008

Image:2hec.jpg


PDB ID 2hec

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Gene: HUMAN LYSOZYME WITH ILE 56 REP (Homo sapiens)
Activity: Lysozyme, with EC number 3.2.1.17
Coordinates: save as pdb, mmCIF, xml



CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY


Contents

Overview

Water molecules frequently occur in the interior of globular proteins. To elucidate the contribution of buried water molecules to the conformational stability of a protein, we examined the crystal structures and the thermodynamic parameters of denaturation of six Ile to Ala/Gly mutant human lysozymes, in which a cavity is created at each mutation site by the substitution of a smaller side-chain for a larger one. One or two ordered water molecules were found in the cavities created in some mutants (I106A, I59A and I59G). The cavity volumes for these three mutants were bigger than those that remained empty in the other mutants. The stability of the mutant proteins with the newly introduced water molecules was about 8 kJ/mol higher than that expected from the change in hydrophobic surface area (DeltaDeltaASAHP) exposed upon denaturation. It was concluded that a water molecule in a cavity created in the interior of a protein contributes favorably to the stability.

Disease

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

About this Structure

2HEC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Contribution of water molecules in the interior of a protein to the conformational stability., Takano K, Funahashi J, Yamagata Y, Fujii S, Yutani K, J Mol Biol. 1997 Nov 21;274(1):132-42. PMID:9398521

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