1HIB

THE STRUCTURE OF AN INTERLEUKIN-1 BETA MUTANT WITH REDUCED BIOACTIVITY SHOWS MULTIPLE SUBTLE CHANGES IN CONFORMATION THAT AFFECT PROTEIN-PROTEIN RECOGNITION

Summary for 1HIB

• Entry DOI: 10.2210/pdb1hib/pdb
• Descriptor: INTERLEUKIN-1 BETA (2 entities in total)
• Functional Keywords: cytokine
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17351.78

Authors

Camacho, N.P.,Smith, D.R.,Goldman, A.,Schneider, B.,Green, D.,Young, P.R.,Berman, H.M. (deposition date: 1993-03-29, release date: 1994-01-31, Last modification date: 2024-02-07)

Primary citation

Camacho, N.P.,Smith, D.R.,Goldman, A.,Schneider, B.,Green, D.,Young, P.R.,Berman, H.M.
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, 1993

PubMed 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.

PubMed: 8364024
DOI: 10.1021/bi00085a005

Experimental method

X-RAY DIFFRACTION (2.4 Å)