1LK2

1.35A crystal structure of H-2Kb complexed with the GNYSFYAL peptide

Summary for 1LK2

• Entry DOI: 10.2210/pdb1lk2/pdb
• Related: 2vaa
• Descriptor: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN, Beta-2-microglobulin, INSULIN RECEPTOR, BETA-SUBUNIT, ... (9 entities in total)
• Functional Keywords: class i mhc-peptide complex, high resolution, anisotropic and tls refinement, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 45324.74

Authors

Luz, J.G.,Rudolph, M.G.,Wilson, I.A.,Eisen, H. (deposition date: 2002-04-23, release date: 2003-11-11, Last modification date: 2024-11-13)

Primary citation

Rudolph, M.G.,Shen, L.Q.,Lamontagne, S.A.,Luz, J.G.,Delaney, J.R.,Ge, Q.,Cho, B.K.,Palliser, D.,McKinley, C.A.,Chen, J.,Wilson, I.A.,Eisen, H.N.
A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: functional and structural aspects.
J.Immunol., 172:2994-3002, 2004

PubMed Abstract: We identify and consider some characteristics of a peptide antagonist for the Ag-specific receptor on 2C cells (the 2C TCR). The peptide, GNYSFYAL (called GNY), binds to H-2K(b), and a very high-resolution crystal structure of the GNY-K(b) complex at 1.35 A is described. Although the GNY peptide does not bind to L(d), the potency of GNY-K(b) as an antagonist is evident from its ability to specifically inhibit 2C TCR-mediated reactions to an allogenic agonist complex (QLSPFPFDL-L(d)), as well as to a syngeneic agonist complex (SIYRYYGL-K(b)). The crystal structure and the activities of alanine-substituted peptide variants point to the properties of the peptide P4 side chain and the conformation of the Tyr-P6 side chain as the structural determinants of GNYSFYAL antagonist activity.

PubMed: 14978103

Experimental method

X-RAY DIFFRACTION (1.35 Å)