1lhh: Difference between revisions
New page: left|200px<br /> <applet load="1lhh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lhh, resolution 1.8Å" /> '''ROLE OF PROLINE RESI... |
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'''ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS'''<br /> | '''ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1LHH 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:// | 1LHH 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=1LHH OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:18:31 2008'' | ||
Revision as of 17:18, 15 February 2008
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ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
OverviewOverview
It has been shown that protein stability can be modulated from, site-directed mutations that affect the entropy of protein unfolding, [Matthews, B. W., Nicholson, H., & Becktel, W. J. (1987) Proc. Natl. Acad., Sci. U.S.A. 84, 6663-6667]. However, the effect of a specific amino acid, replacement on stability highly depends on the location of the mutation, site and its environment in the protein structure [Yutani, K., Hayashi, S., Sugisaki, Y., & Ogasahara, K. (1991) Proteins Struct., Funct., Genet., 9, 90-98). To clarify the role of specific proline residues in the, thermostability of human lysozyme (h-lysozyme), a series of proline, mutants were investigated by means of scanning calorimetry and, high-resolution X-ray crystallography. The thermodynamic properties of the, mutant and wild-type h-lysozymes are compared and discussed on the basis, of their three-dimensional structure. h-Lysozyme contains two proline, residues at positions 71 and 103. The Pro71----Gly substitution was found, to destabilize h-lysozyme by decreasing the entropic contribution of, unfolding by about 2 kcal/mol at 68.8 degrees C. This is consistent with, the theoretical expectations for such a substitution. However, the same, substitution at position 103 (Pro103----Gly) does not affect h-lysozyme, stability, and the thermodynamic properties of the P71G/P103G and P71G, mutants are essentially the same. Pro71 which is conserved among lysozymes, from other species, appears to be important for stability, whereas Pro103, which is not conserved, does not. These differences are explained in terms, of residue accessibility to the solvent and crystallographic B-factor, which reflects the amino acid mobility.(ABSTRACT TRUNCATED AT 250 WORDS)
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1LHH is a Single protein structure of sequence from Homo sapiens. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants., Herning T, Yutani K, Inaka K, Kuroki R, Matsushima M, Kikuchi M, Biochemistry. 1992 Aug 11;31(31):7077-85. PMID:1643041
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