Recombinant expression and partial characterization of the human formyl peptide receptor

A Lala; A Sharma; H T Sojar; S J Radel; R J Genco; E De Nardin

doi:10.1016/0167-4889(93)90208-7

Recombinant expression and partial characterization of the human formyl peptide receptor

Biochim Biophys Acta. 1993 Sep 13;1178(3):302-6. doi: 10.1016/0167-4889(93)90208-7.

Authors

A Lala¹, A Sharma, H T Sojar, S J Radel, R J Genco, E De Nardin

Affiliation

¹ Department of Oral Biology, School of Dentistry, State University of New York at Buffalo 14214.

PMID: 8364044
DOI: 10.1016/0167-4889(93)90208-7

Abstract

FMLP-receptor DNA was expressed in Escherichia coli. The expressed product could specifically bind FMLP. This is the first-reported expression of a functional FMLP receptor in Escherichia coli. We confirm that receptor glycosylation is not essential for ligand binding. A deletion mutant did not bind FMLP, suggesting that the deleted portion plays a role in ligand binding.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Base Sequence
Escherichia coli / genetics*
Escherichia coli / metabolism
Humans
Models, Molecular
Molecular Sequence Data
Receptors, Formyl Peptide
Receptors, Immunologic / biosynthesis*
Receptors, Immunologic / chemistry
Recombinant Proteins / biosynthesis*

Substances

Receptors, Formyl Peptide
Receptors, Immunologic
Recombinant Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding