dc.contributor.author |
Nolte, M |
en |
dc.contributor.author |
Pepinsky, R |
en |
dc.contributor.author |
Venyaminov, S |
en |
dc.contributor.author |
Koteliansky, V |
en |
dc.contributor.author |
Gotwals, P |
en |
dc.contributor.author |
Karpusas, M |
en |
dc.date.accessioned |
2014-06-06T06:43:52Z |
|
dc.date.available |
2014-06-06T06:43:52Z |
|
dc.date.issued |
1999 |
en |
dc.identifier.uri |
http://dx.doi.org/10.1016/S0014-5793(99)00666-3 |
en |
dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/1517 |
|
dc.subject |
Absorption Spectra |
en |
dc.subject |
Cell Surface |
en |
dc.subject |
Crystal Structure |
en |
dc.subject |
Domain Structure |
en |
dc.subject |
Ligand Binding |
en |
dc.subject |
Metal Ion |
en |
dc.subject |
Amino Acid |
en |
dc.subject |
Circular Dichroism |
en |
dc.title |
Crystal structure of the α1β1 integrin I-domain: insights into integrin I-domain function |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1016/S0014-5793(99)00666-3 |
en |
heal.publicationDate |
1999 |
en |
heal.abstract |
The α1β1 integrin is a major cell surface receptor for collagen. Ligand binding is mediated, in part, through a ∼200 amino acid inserted ‘I’-domain contained in the extracellular part of the integrin α chain. Integrin I-domains contain a divalent cation binding (MIDAS) site and require cations to interact with integrin ligands. We have determined the crystal structure of recombinant I-domain |
en |
heal.journalName |
Febs Letters |
en |
dc.identifier.doi |
10.1016/S0014-5793(99)00666-3 |
en |