CHEBI:76630 - N⁶-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine

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ChEBI Name N6-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine ChEBI ID CHEBI:76630 ChEBI ASCII Name N(6)-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine Definition A D-lysine derivative in which D-lysine is substituted on N6 by a (2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl group. Stars This entity has been manually annotated by the ChEBI Team. Supplier Information ZINC000096095489 Download Molfile XML SDF Find compounds which contain this structure Find compounds which resemble this structure Take structure to the Advanced Search Formula C13H19N7O3 Net Charge 0 Average Mass 321.33510 Monoisotopic Mass 321.15494 InChI InChI=1S/C13H19N7O3/c14-8(12(22)23)3-1-2-4-16-5-7-6-17-10-9(18-7)11(21)20-13(15)19-10/h6,8,16H,1-5,14H2,(H,22,23)(H3,15,17,19,20,21)/t8-/m1/s1 InChIKey VSWOPALBOJUOOW-MRVPVSSYSA-N SMILES N[C@H](CCCCNCc1cnc2nc(N)[nH]c(=O)c2n1)C(O)=O Roles Classification Chemical Role(s): Bronsted base A molecular entity capable of accepting a hydron from a donor (Bronsted acid). (via organic amino compound ) Bronsted acid A molecular entity capable of donating a hydron to an acceptor (Bronsted base). (via oxoacid ) View more via ChEBI Ontology ChEBI Ontology Outgoing N6-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine (CHEBI:76630) has functional parent 2-aminopteridin-4(3H)-one (CHEBI:44992) N6-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine (CHEBI:76630) is a D-α-amino acid (CHEBI:16733) N6-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine (CHEBI:76630) is a D-lysine derivative (CHEBI:76632) IUPAC Name N6-[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]-D-lysine Synonyms Sources (2R)-2-amino-6-{[(2-amino-4-oxo-3,4-dihydropteridin-6-yl)methyl]amino}hexanoic acid IUPAC (2R)-2-azanyl-6-[(2-azanyl-4-oxidanylidene-3H-pteridin-6-yl)methylamino]hexanoic acid PDBeChem Manual Xref Database KFP PDBeChem View more database links Citation López-Sagaseta J, Dulberger CL, McFedries A, Cushman M, Saghatelian A, Adams EJ (2013) MAIT recognition of a stimulatory bacterial antigen bound to MR1. Journal of immunology (Baltimore, Md. : 1950) 191, 5268-5277 [PubMed:24108697] [show Abstract] MR1-restricted mucosal-associated invariant T (MAIT) cells represent a subpopulation of αβ T cells with innate-like properties and limited TCR diversity. MAIT cells are of interest because of their reactivity against bacterial and yeast species, suggesting that they play a role in defense against pathogenic microbes. Despite the advances in understanding MAIT cell biology, the molecular and structural basis behind their ability to detect MR1-Ag complexes is unclear. In this study, we present our structural and biochemical characterization of MAIT TCR engagement of MR1 presenting an Escherichia coli-derived stimulatory ligand, rRL-6-CH2OH, previously found in Salmonella typhimurium. We show a clear enhancement of MAIT TCR binding to MR1 due to the presentation of this ligand. Our structure of a MAIT TCR/MR1/rRL-6-CH2OH complex shows an evolutionarily conserved binding orientation, with a clear role for both the CDR3α and CDR3β loops in recognizing the rRL-6-CH2OH stimulatory ligand. We also present two additional xenoreactive MAIT TCR/MR1 complexes that recapitulate the docking orientation documented previously, despite having variation in the CDR2β and CDR3β loop sequences. Our data support a model by which MAIT TCRs engage MR1 in a conserved fashion, with their binding affinities modulated by the nature of the MR1-presented Ag or diversity introduced by alternate Vβ usage or CDR3β sequences. Last Modified 16 December 2014