1ip6: Difference between revisions
New page: left|200px<br /> <applet load="1ip6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ip6, resolution 1.8Å" /> '''G127A HUMAN LYSOZYME... |
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[[Image:1ip6. | [[Image:1ip6.jpg|left|200px]]<br /><applet load="1ip6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''G127A HUMAN LYSOZYME'''<br /> | '''G127A HUMAN LYSOZYME'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1IP6 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]. 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:// | 1IP6 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=1IP6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: glycosidase]] | [[Category: glycosidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:03:04 2008'' | ||
Revision as of 17:03, 15 February 2008
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G127A HUMAN LYSOZYME
OverviewOverview
Our previous study of six non-Gly to Gly/Ala mutant human lysozymes in a, left-handed helical region showed that only one non-Gly residue at a rigid, site had unfavorable strain energy as compared with Gly at the same, position (Takano et al., Proteins 2001; 44:233-243). To further examine, the role of left-handed residues in the conformational stability of a, protein, we constructed ten Gly to Ala mutant human lysozymes. Most Gly, residues in human lysozyme are located in the left-handed helix region., The thermodynamic parameters for denaturation and crystal structures were, determined by differential scanning calorimetry and X-ray analysis, respectively. The difference in denaturation Gibbs energy (DeltaDeltaG), for the ten Gly to Ala mutants ranged from + 1.9 to -7.5 kJ/mol, indicating that the effect of the mutation depends on the environment of, the residue. We confirm that Gly in a left-handed region is more favorable, at rigid sites than non-Gly, but there is little difference in energetic, cost between Gly and non-Gly at flexible sites. The present results, indicate that dihedral angles in the backbone conformation and also the, flexibility at the position should be considered for analyses of protein, stability, and protein structural determination, prediction, and design.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1IP6 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
ReferenceReference
Role of amino acid residues in left-handed helical conformation for the conformational stability of a protein., Takano K, Yamagata Y, Yutani K, Proteins. 2001 Nov 15;45(3):274-80. PMID:11599030
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