PDBsum entry: 1too

Immune system

PDB id: 1too

Contents

Protein chain

153 a.a. *

Waters ×75

* Residue conservation analysis

PDB id:

1too

Name:

Immune system

Title:

Interleukin 1b mutant f146w

Structure:

Interleukin-1 beta. Chain: a. Synonym: il-1 beta, catabolin. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: il1b. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.10Å R-factor: 0.185 R-free: 0.199

Authors:

D.H.Adamek,L.Guerrero,D.L.Caspar

Key ref:

D.H.Adamek et al. (2005). Structural and energetic consequences of mutations in a solvated hydrophobic cavity. J Mol Biol, 346, 307-318. PubMed id: 15663946 DOI: 10.1016/j.jmb.2004.11.046

Date:

14-Jun-04 Release date: 07-Dec-04

Protein chain

P01584  (IL1B_HUMAN) -  Interleukin-1 beta

Seq: 269 a.a.

Struc: 153 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (2 terms)
• Biological process: immune response (2 terms)
• Biochemical function: growth factor activity (2 terms)

DOI no: 10.1016/j.jmb.2004.11.046

J Mol Biol 346:307-318 (2005)

PubMed id: 15663946

Structural and energetic consequences of mutations in a solvated hydrophobic cavity.

D.H.Adamek, L.Guerrero, M.Blaber, D.L.Caspar.

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.

Selected figure(s)

Figure 1.
Figure 1. Ball and stick diagram of the cavity residues of wild-type Il-1b. The wire contour represents positionally disordered water observed crystallographically. The triad of phenylalanine residues that circumscribe the cavity are shown in gray. Phenylalanine 101 (dark gray) is not solvent-accessible from the cavity. All other residues shown in light grey are the residues that form the cavity. Image adapted from Yu et al.2

Figure 5.
Figure 5. Local structure of F101Y around the mutation site. The stereograph ball and stick model of the mutant structure is shown superposed over the darker, smaller, wild-type structure. Large dark spheres represent water molecules. Dotted lines represent putative hydrogen bonds.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 346, 307-318) copyright 2005.

Figures were selected by an automated process.