1EIS

UDA UNCOMPLEXED FORM. CRYSTAL STRUCTURE OF URTICA DIOICA AGGLUTININ, A SUPERANTIGEN PRESENTED BY MHC MOLECULES OF CLASS I AND CLASS II

Summary for 1EIS

• Entry DOI: 10.2210/pdb1eis/pdb
• Related: 1EN2 1ENM
• Descriptor: PROTEIN (AGGLUTININ ISOLECTIN VI/AGGLUTININ ISOLECTIN V) (2 entities in total)
• Functional Keywords: lectin, hevein domain, uda, superantigen, sugar binding protein
• Biological source: Urtica dioica (great nettle)
• Total number of polymer chains: 1
• Total formula weight: 9350.27

Authors

Saul, F.A.,Rovira, P.,Boulot, G.,Van Damme, E.J.M.,Peumans, W.J.,Truffa-Bachi, P.,Bentley, G.A. (deposition date: 2000-02-28, release date: 2000-06-21, Last modification date: 2024-10-30)

Primary citation

Saul, F.A.,Rovira, P.,Boulot, G.,Damme, E.J.,Peumans, W.J.,Truffa-Bachi, P.,Bentley, G.A.
Crystal structure of Urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II.
Structure Fold.Des., 8:593-603, 2000

PubMed Abstract: Urtica dioica agglutinin (UDA), a monomeric lectin extracted from stinging nettle rhizomes, is specific for saccharides containing N-acetylglucosamine (GlcNAc). The lectin behaves as a superantigen for murine T cells, inducing the exclusive proliferation of Vbeta8.3(+) lymphocytes. UDA is unique among known T cell superantigens because it can be presented by major histocompatibility complex (MHC) molecules of both class I and II.

PubMed: 10873861
DOI: 10.1016/S0969-2126(00)00142-8

Experimental method

X-RAY DIFFRACTION (1.66 Å)