1gfh: Difference between revisions
New page: left|200px<br /> <applet load="1gfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gfh, resolution 1.8Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1gfh. | [[Image:1gfh.jpg|left|200px]]<br /><applet load="1gfh" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1gfh" size=" | |||
caption="1gfh, resolution 1.8Å" /> | caption="1gfh, resolution 1.8Å" /> | ||
'''CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS'''<br /> | '''CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1GFH 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:// | 1GFH 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=1GFH OCA]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: surface]] | [[Category: surface]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:53:20 2008'' | ||
Revision as of 16:53, 15 February 2008
|
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
1GFH 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
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
Page seeded by OCA on Fri Feb 15 15:53:20 2008