| dc.contributor.author |
Karpusas, M |
en |
| dc.contributor.author |
Ferrant, J |
en |
| dc.contributor.author |
Weinreb, P |
en |
| dc.contributor.author |
Carmillo, A |
en |
| dc.contributor.author |
Taylor, F |
en |
| dc.contributor.author |
Garber, E |
en |
| dc.date.accessioned |
2014-06-06T06:45:19Z |
|
| dc.date.available |
2014-06-06T06:45:19Z |
|
| dc.date.issued |
2003 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/S0022-2836(03)00203-1 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/2361 |
|
| dc.subject |
Binding Affinity |
en |
| dc.subject |
Binding Site |
en |
| dc.subject |
Cell Surface |
en |
| dc.subject |
Crystal Structure |
en |
| dc.subject |
Glutamate |
en |
| dc.subject |
Metal Ion |
en |
| dc.subject |
Monoclonal Antibody |
en |
| dc.subject |
Root Mean Square |
en |
| dc.subject |
Complementarity Determining Region |
en |
| dc.subject |
Heavy Chain |
en |
| dc.title |
Crystal Structure of the α1β1 Integrin I Domain in Complex with an Antibody Fab Fragment |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/S0022-2836(03)00203-1 |
en |
| heal.publicationDate |
2003 |
en |
| heal.abstract |
The α1β1 (VLA-1) integrin is a cell-surface receptor for collagen and laminin and has been implicated in biological pathways involved in several pathological processes. These processes may be inhibited by the monoclonal antibody AQC2, which binds with high affinity to human α1β1 integrin. To understand the structural basis of the inhibition we determined the crystal structure of the complex of |
en |
| heal.journalName |
Journal of Molecular Biology |
en |
| dc.identifier.doi |
10.1016/S0022-2836(03)00203-1 |
en |