1too: Difference between revisions
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[[Image:1too.jpg|left|200px]] | [[Image:1too.jpg|left|200px]] | ||
'''Interleukin 1B Mutant F146W''' | {{Structure | ||
|PDB= 1too |SIZE=350|CAPTION= <scene name='initialview01'>1too</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= IL1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Interleukin 1B Mutant F146W''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TOO is a [ | 1TOO is a [[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=1TOO OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15663946 15663946] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrophobicity]] | [[Category: hydrophobicity]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:21:13 2008'' | ||
Revision as of 15:21, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Gene: | IL1B (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Interleukin 1B Mutant F146W
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Gastric cancer risk after H. pylori infection OMIM:[147720]
About this StructureAbout this Structure
1TOO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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