The human integrin very late antigen (VLA)-2 (CD49b/CD29) mediates interactions with
collagen and is the receptor for echovirus 1. Binding sites for both collagen and echovirus 1 …

VLA-2, the α2β1 integrin, mediates cell adhesion to collagen and laminin, and is the
receptor for the human pathogen echovirus 1. Because of its similarity to domains present in …

Human VLA-2 (α2β1) mediates cellular adhesion to collagen and laminin and cell
attachment by the human pathogen echovirus 1. We report here the cloning, sequencing …

The integrin VLA-2 mediates cell adhesion to collagen and laminin and also functions as a
virus receptor, mediating cell surface attachment and infection by a human pathogen …

We have determined the high resolution crystal structure of the I domain from the α-subunit
of the integrin α2β1, a cell surface adhesion receptor for collagen and the human pathogen …

Conformational activation increases the affinity of integrins to their ligands. On ligand
binding, further changes in integrin conformation elicit cellular signalling. Unlike any of the …

Integrins are cell surface receptors for several microbial pathogens including echovirus 1
(EV1), a picornavirus. Cryo-electron microscopy revealed that the functional domain (α 2 I) of …

The isolated I domain of the integrin VLA-2, produced as a bacterial fusion protein,
specifically bound echovirus 1 and prevented virus attachment to cells. These results …

Integrin alpha 2 beta 1 is a cell surface adhesion receptor for collagen and echovirus 1.
Here we localized the epitopes for anti-alpha 2 monoclonal antibodies using interspecies …

The α 1 β 1 and α 2 β 1 integrins are cell surface collagen receptors. Cells expressing the α
1 β 1 integrin preferentially adhere to collagen IV, whereas cells expressing the α 2 β 1 …