1gfr

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Revision as of 17:58, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1gfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gfr, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF...)
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File:1gfr.gif


1gfr, resolution 1.8Å

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CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS

OverviewOverview

Water molecules make a hydration structure with the network of hydrogen, bonds, covering on the surface of proteins. To quantitatively estimate the, contribution of the hydration structure to protein stability, a series of, hydrophilic mutant human lysozymes (Val to Ser, Tyr, Asp, Asn, and Arg), modified at three different positions on the surface, which are located in, the alpha-helix (Val-110), the beta-sheet (Val-2), and the loop (Val-74), were constructed. Their thermodynamic parameters of denaturation and, crystal structures were examined by calorimetry and by x-ray, crystallography at 100 K, respectively. The introduced polar residues made, hydrogen bonds with protein atoms and/or water molecules, sometimes, changing the hydration structure around the mutation site. Changes in the, stability of the mutant proteins can be evaluated by a unique equation, that considers the conformational changes resulting from the, substitutions. Using this analysis, the relationship between the changes, in the stabilities and the hydration structures for mutant human lysozymes, substituted on the surface could be quantitatively estimated. The analysis, indicated that the hydration structure on protein surface plays an, important role in determining the conformational stability of the protein.

DiseaseDisease

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

About this StructureAbout this Structure

1GFR is a Single protein structure of sequence from Homo sapiens with NA as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability., Funahashi J, Takano K, Yamagata Y, Yutani K, J Biol Chem. 2002 Jun 14;277(24):21792-800. Epub 2002 Apr 1. PMID:11927576

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