1t4q

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{{STRUCTURE_1t4q| PDB=1t4q | SCENE= }}
{{STRUCTURE_1t4q| PDB=1t4q | SCENE= }}
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'''Interleukin 1 beta F101W'''
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===Interleukin 1 beta F101W===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15663946 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15663946}}
==Disease==
==Disease==
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[[Category: Il-1b]]
[[Category: Il-1b]]
[[Category: Il1b]]
[[Category: Il1b]]
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Revision as of 05:16, 29 July 2008

Image:1t4q.png

Template:STRUCTURE 1t4q

Contents

Interleukin 1 beta F101W

Template:ABSTRACT PUBMED 15663946

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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