1twm: Difference between revisions

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[[Image:1twm.gif|left|200px]]
[[Image:1twm.gif|left|200px]]


{{Structure
<!--
|PDB= 1twm |SIZE=350|CAPTION= <scene name='initialview01'>1twm</scene>, resolution 2.26&Aring;
The line below this paragraph, containing "STRUCTURE_1twm", creates the "Structure Box" on the page.
|SITE=
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|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= IL1B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_1twm|  PDB=1twm |  SCENE= }}  
|RELATEDENTRY=[[1s0l|1S0L]], [[1twe|1TWE]], [[1t4q|1T4Q]], [[1too|1TOO]], [[1tp0|1TP0]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1twm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1twm OCA], [http://www.ebi.ac.uk/pdbsum/1twm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1twm RCSB]</span>
}}


'''Interleukin-1 Beta Mutant F146Y'''
'''Interleukin-1 Beta Mutant F146Y'''
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[[Category: Adamek, D H.]]
[[Category: Adamek, D H.]]
[[Category: Capsar, D L.]]
[[Category: Capsar, D L.]]
[[Category: hydrophobic cavity]]
[[Category: Hydrophobic cavity]]
[[Category: hydrophobicity]]
[[Category: Hydrophobicity]]
[[Category: solvation]]
[[Category: Solvation]]
[[Category: water]]
[[Category: Water]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:02:07 2008''

Revision as of 10:27, 3 May 2008

File:1twm.gif

Template:STRUCTURE 1twm

Interleukin-1 Beta Mutant F146Y


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

1TWM 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 Page seeded by OCA on Sat May 3 10:27:38 2008

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