1t4q
From Proteopedia
(New page: 200px<br /> <applet load="1t4q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t4q, resolution 2.1Å" /> '''Interleukin 1 beta F...) |
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caption="1t4q, resolution 2.1Å" /> | caption="1t4q, resolution 2.1Å" /> | ||
'''Interleukin 1 beta F101W'''<br /> | '''Interleukin 1 beta F101W'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1T4Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1T4Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T4Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: il1b]] | [[Category: il1b]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:55:21 2008'' |
Revision as of 14:55, 15 February 2008
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Interleukin 1 beta F101W
Contents |
Overview
The structural and energetic consequences of modifications to the, hydrophobic cavity of interleukin 1-beta (IL-1beta) are described., Previous reports demonstrated that the entirely hydrophobic cavity of, IL-1beta contains positionally disordered water. To gain a better, understanding of the nature of this cavity and the water therein, a number, of mutant proteins were constructed by site-directed mutagenesis, designed, to result in altered hydrophobicity of the cavity. These mutations involve, the replacement of specific phenylalanine residues, which circumscribe the, cavity, with tyrosine, tryptophan, leucine and isoleucine. Using, differential scanning calorimetry to determine the relative stabilities of, the wild-type and mutant proteins, we found all of the mutants to be, destabilizing. X-ray crystallography was used to identify the structural, consequences of the mutations. No clear correlation between the, hydrophobicities of the specific side-chains introduced and the resulting, stabilities was found.
Disease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this Structure
1T4Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and energetic consequences of mutations in a solvated hydrophobic cavity., Adamek DH, Guerrero L, Blaber M, Caspar DL, J Mol Biol. 2005 Feb 11;346(1):307-18. Epub 2004 Dec 24. PMID:15663946
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