1b7l

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Revision as of 17:00, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1b7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7l, resolution 1.8Å" /> '''VERIFICATION OF SPMP...)
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File:1b7l.gif


1b7l, resolution 1.8Å

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VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

OverviewOverview

The stability profile of mutant protein (SPMP) (Ota,M., Kanaya,S. and, Nishikawa,K., 1995, J. Mol. Biol., 248, 733-738) estimates the changes in, conformational stability due to single amino acid substitutions using a, pseudo-energy potential developed for evaluating structure-sequence, compatibility in the structure prediction method, the 3D-1D compatibility, evaluation. Nine mutant human lysozymes expected to significantly increase, in stability from SPMP were constructed, in order to experimentally verify, the reliability of SPMP. The thermodynamic parameters for denaturation and, crystal structures of these mutant proteins were determined. One mutant, protein was stabilized as expected, compared with the wild-type protein., However, the others were not stabilized even though the structural changes, were subtle, indicating that SPMP overestimates the increase in stability, or underestimates negative effects due to substitution. The stability, changes in the other mutant human lysozymes previously reported were also, analyzed by SPMP. The correlation of the stability changes between the, experiment and prediction depended on the types of substitution: there, were some correlations for proline mutants and cavity-creating mutants, but no correlation for mutants related to side-chain hydrogen bonds. The, present results may indicate some additional factors that should be, considered in the calculation of SPMP, suggesting that SPMP can be refined, further.

DiseaseDisease

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

About this StructureAbout this Structure

1B7L 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

Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes., Takano K, Ota M, Ogasahara K, Yamagata Y, Nishikawa K, Yutani K, Protein Eng. 1999 Aug;12(8):663-72. PMID:10469827

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