N-terminal-methionylated interleukin-1 beta has reduced receptor-binding affinity

P Wingfield; P Graber; N R Movva; A M Gronenborn; G M Clore; H R MacDonald

doi:10.1016/0014-5793(87)80133-3

N-terminal-methionylated interleukin-1 beta has reduced receptor-binding affinity

FEBS Lett. 1987 May 4;215(1):160-4. doi: 10.1016/0014-5793(87)80133-3.

Authors

P Wingfield, P Graber, N R Movva, A M Gronenborn, G M Clore, H R MacDonald

PMID: 2952523
DOI: 10.1016/0014-5793(87)80133-3

Abstract

The receptor-binding affinity of recombinant-derived interleukin-1 beta containing unprocessed N-terminal methionine (MAPV-) was 10-fold lower than protein containing the authentic N-terminal sequence (APV-). Structural analysis of the methionylated and non-methionylated proteins by NMR spectroscopy detected no (or minor) conformational differences. The differences in binding affinity, therefore, suggest that the additional N-terminal methionine causes a small, direct or indirect, perturbation of the receptor-binding region.

Publication types

Comparative Study

MeSH terms

Escherichia coli / metabolism
Interleukin-1 / analogs & derivatives
Interleukin-1 / metabolism*
N-Formylmethionine / metabolism
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Receptors, Immunologic / metabolism*
Receptors, Interleukin-1
Recombinant Proteins / metabolism

Substances

Interleukin-1
Receptors, Immunologic
Receptors, Interleukin-1
Recombinant Proteins
N-Formylmethionine