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Abstract
The Structure of the β-Propeller Domain and C-terminal Region of the Integrin αM Subunit: DEPENDENCE ON β SUBUNIT ASSOCIATION AND PREDICTION OF DOMAINS
Highlights
The integrin family of adhesion molecules participate in important cell-cell and cell-extracellular matrix interactions in a diverse range of biological processes [1]
Electron microscopic images of integrins reveal that the N-terminal portions of the ␣ and  subunits fold into a globular head that is connected to the membrane by two rodlike segments about 16 nm long corresponding to the C-terminal portions of the ␣ and  extracellular domains (20 –22)
MAbs to the -Propeller Domain and a Subset of monoclonal antibodies (mAbs) to the C-terminal Region Do Not React with the Unassociated ␣M Subunit—To study whether folding of the ␣M subunit is dependent on association with the 2 subunit, we examined the expression of mAb epitopes on the unassociated ␣M subunit
Summary
The integrin family of adhesion molecules participate in important cell-cell and cell-extracellular matrix interactions in a diverse range of biological processes [1]. The integrin  subunits contain a conserved domain of about 250 amino acids in the N-terminal portion This domain has been predicted to have an “I-domainlike” fold [14, 18, 19]. Since mAbs specific for the region of the ␣L subunit C-terminal to the -propeller domain have not been described, it is not known whether folding of this region is dependent on association with the  subunit. Compared with the previous studies on LFA-1, our studies on the -propeller domain are more definitive, since mAb specificity is defined to individual amino acid substitutions between mouse and human, and mAb to epitopes that are widely separated in the predicted -propeller structure all show a dependence on  subunit association for reactivity. Much of the C-terminal region of the ␣M subunit appears to assume a native fold independently of association with the 2 subunit
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