1b7s: Difference between revisions
New page: left|200px<br /> <applet load="1b7s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7s, resolution 2.Å" /> '''VERIFICATION OF SPMP ... |
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[[Image:1b7s.gif|left|200px]]<br /> | [[Image:1b7s.gif|left|200px]]<br /><applet load="1b7s" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1b7s, resolution 2.Å" /> | caption="1b7s, resolution 2.Å" /> | ||
'''VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES'''<br /> | '''VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES'''<br /> | ||
==Overview== | ==Overview== | ||
The stability profile of mutant protein (SPMP) (Ota,M., Kanaya,S. and | 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. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1B7S 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 NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1B7S 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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7S OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: mutant stability]] | [[Category: mutant stability]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:28 2008'' | ||
Revision as of 12:52, 21 February 2008
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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
1B7S is a Single protein structure of sequence from Homo sapiens with as ligand. 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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