1TOO

Interleukin 1B Mutant F146W

1TOO の概要

• エントリーDOI: 10.2210/pdb1too/pdb
• 関連するPDBエントリー: 1S0L 1T4Q 1TP0 1TWE 1TWM
• 分子名称: Interleukin-1 beta (2 entities in total)
• 機能のキーワード: hydrophobic cavity, hydrophobicity, immune system
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytosol : P01584
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17434.87

構造登録者

Adamek, D.H.,Guerrero, L.,Caspar, D.L. (登録日: 2004-06-14, 公開日: 2004-12-07, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)