1TOO

Interleukin 1B Mutant F146W

Summary for 1TOO

• Entry DOI: 10.2210/pdb1too/pdb
• Related: 1S0L 1T4Q 1TP0 1TWE 1TWM
• Descriptor: Interleukin-1 beta (2 entities in total)
• Functional Keywords: hydrophobic cavity, hydrophobicity, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol : P01584
• Total number of polymer chains: 1
• Total formula weight: 17434.87

Authors

Adamek, D.H.,Guerrero, L.,Caspar, D.L. (deposition date: 2004-06-14, release date: 2004-12-07, Last modification date: 2024-02-14)

Primary citation

Adamek, D.H.,Guerrero, L.,Blaber, M.,Caspar, D.L.
Structural and energetic consequences of mutations in a solvated hydrophobic cavity.
J.Mol.Biol., 346:307-318, 2005

PubMed Abstract: 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.

PubMed: 15663946
DOI: 10.1016/j.jmb.2004.11.046

Experimental method

X-RAY DIFFRACTION (2.1 Å)