Conformation, stability, and folding of interleukin 1 beta.


Abstract

Recombinant human interleukin 1 beta has been studied in solution with respect to its conformation, stability, and characteristics of unfolding and refolding. It is an all-beta-type, stable globular protein with a high cooperativity under conditions where refolding is reversible. The tryptophan residue is approximately 40% exposed to solvent, and the four tyrosines are 50% exposed. The fluorescence of the single tryptophan residue is quenched at pH 7.5 but dequenched by high salt, by titration to lower pH with a pK of 6.59, and by denaturants, resulting in an unusual biphasic change in fluorescence on unfolding. Both histidine and thiol residues have been excluded as being responsible for the pH dependence of fluorescence by site-directed mutagenesis and by chemical modification, respectively. The likely candidate is an aspartate or glutamate. Study holds ProTherm entries: 3866 Extra Details: all-beta-type; cooperativity ; biphasic change;,chemical modification

Submission Details

ID: yFsipxN

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:23 p.m.

Version: 1

Publication Details
Craig S;Schmeissner U;Wingfield P;Pain RH,Biochemistry (1987) Conformation, stability, and folding of interleukin 1 beta. PMID:3498512
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1HIB 1993-03-29T00:00:00+0000 2.4 THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION
1I1B 1989-12-05T00:00:00+0000 2.0 CRYSTAL STRUCTURE OF RECOMBINANT HUMAN INTERLEUKIN-1BETA AT 2.0 ANGSTROMS RESOLUTION
1IOB 1996-03-14T00:00:00+0000 2.0 INTERLEUKIN-1 BETA FROM JOINT X-RAY AND NMR REFINEMENT
1ITB 1997-01-15T00:00:00+0000 2.5 TYPE-1 INTERLEUKIN-1 RECEPTOR COMPLEXED WITH INTERLEUKIN-1 BETA
1L2H 2002-02-21T00:00:00+0000 1.54 Crystal structure of Interleukin 1-beta F42W/W120F mutant
1S0L 2003-12-31T00:00:00+0000 2.34 Interleukin 1 beta mutant F42W
1T4Q 2004-04-30T00:00:00+0000 2.1 Interleukin 1 beta F101W
1TOO 2004-06-14T00:00:00+0000 2.1 Interleukin 1B Mutant F146W
1TP0 2004-06-15T00:00:00+0000 2.2 Triple mutation in interleukin 1 beta cavity:replacement of phenylalanines with tryptophan.
1TWE 2004-06-30T00:00:00+0000 2.1 INTERLEUKIN 1 BETA MUTANT F101Y

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
94.8 Interleukin-1 beta P46648 IL1B_CERAT
95.4 Interleukin-1 beta P79182 IL1B_MACFA
95.4 Interleukin-1 beta P51493 IL1B_MACNE
96.1 Interleukin-1 beta P48090 IL1B_MACMU
100.0 Interleukin-1 beta P01584 IL1B_HUMAN