Purification and structural characterization of the CD11b/CD18 integrin α subunit I domain reveals a folded conformation in solution

The α subunits of the leukocyte CD11/CD18 integrins contain a ∼200 amino acid ‘inserted’ or I domain. The I domain of the cell-surface Mac-1(CD11b/CD18) integrin has been shown to be the major recognition site for several adhesion ligands, including iC3b, fibrinogen, factor X, and ICAM-1. The I doma...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1995-08, Vol.369 (2), p.197-201
Main Authors: Fairbanks, Michael B., Pollock, John R., Prairie, Mark D., Scahill, Terrence A., Baczynskyj, Lubo, Heinrikson, Robert L., Stockman, Brian J.
Format: Article
Language:English
Subjects:
Adhesion biology
Amino Acid Sequence
Amino Acids - analysis
Calcium - pharmacology
CD18 Antigens - chemistry
CD18 Antigens - isolation & purification
Circular Dichroism
Escherichia coli - genetics
Factor Xa
Fusion protein
Glutathione Transferase - genetics
I domain
Integrin
Leukocytes - chemistry
Macrophage-1 Antigen - chemistry
Macrophage-1 Antigen - isolation & purification
Magnesium - pharmacology
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Protein Conformation - drug effects
Protein Folding
Protein NMR
Recombinant Fusion Proteins - biosynthesis
Recombinant Fusion Proteins - isolation & purification
Sequence Analysis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The α subunits of the leukocyte CD11/CD18 integrins contain a ∼200 amino acid ‘inserted’ or I domain. The I domain of the cell-surface Mac-1(CD11b/CD18) integrin has been shown to be the major recognition site for several adhesion ligands, including iC3b, fibrinogen, factor X, and ICAM-1. The I domain from the Mac-1 α subunit has been expressed in Escherichia coli as a soluble GST-fusion protein containing a factor X a sensitive cleavage site. Analytical characterization of the purified I domain reveals that it is obtained in very high quality at high yields. CD and NMR spectra indicate that I domain adopts a predominantly folded structure in solution, independent of the remainder of the α subunit. Addition of Ca 2+ and Mg 2+ did not significantly perturb the structural conformation.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00747-W