PDBsum entry: 1hib

Cytokine

PDB id: 1hib

Contents

Protein chain

150 a.a. *

Waters ×113

* Residue conservation analysis

PDB id:

1hib

Name:

Cytokine

Title:

The structure of an interleukin-1 beta mutant with reduced b shows multiple subtle changes in conformation that affect p protein recognition

Structure:

Interleukin-1 beta. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

Biol. unit:

Dimer (from PQS)

Resolution:

2.40Å R-factor: 0.190

Authors:

N.P.Camacho,D.R.Smith,A.Goldman,B.Schneider,D.Green,P.R.Youn H.M.Berman

Key ref:

N.P.Camacho et al. (1993). Structure of an interleukin-1 beta mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition. Biochemistry, 32, 8749-8757. PubMed id: 8364024 DOI: 10.1021/bi00085a005

Date:

29-Mar-93 Release date: 31-Jan-94

Protein chain

P01584  (IL1B_HUMAN) -  Interleukin-1 beta

Seq: 269 a.a.

Struc: 150 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: 10.1021/bi00085a005

Biochemistry 32:8749-8757 (1993)

PubMed id: 8364024

Structure of an interleukin-1 beta mutant with reduced bioactivity shows multiple subtle changes in conformation that affect protein-protein recognition.

N.P.Camacho, D.R.Smith, A.Goldman, B.Schneider, D.Green, P.R.Young, H.M.Berman.

ABSTRACT

Site-specific mutagenesis was used to obtain the human interleukin-1 beta mutant protein with glycine substituted for threonine at position 9 (IL-1 beta Thr9Gly). The mutant maintains receptor binding but exhibits significantly reduced biological activity. The crystal structure of IL-1 beta Thr9Gly has been determined at 2.4-A resolution by molecular replacement techniques and refined to a crystallographic R-factor of 19.0%. IL-1 beta Thr9Gly crystallizes in a different space group (P6(5)22) than does native IL-1 beta (P4(3)); thus the molecules pack differently. Their overall structure is similar, nevertheless, with both composed of 153 amino acids which form 12 antiparallel beta-strands. However, significant conformational differences both close to and far from the site of the mutation may explain the mutant's altered properties.