Characterization of αX I-Domain Binding to Receptors for Advanced Glycation End Products (RAGE).

) and shows an affinity on the sub-micro molar level: the dissociation constant of αX I-domains binding to being 0.49 μM. Furthermore, the αX I-domains recognize the V-domain, but not the C1 and C2-domains of The acidic amino acid substitutions on the ligand binding site of αX I-domain significantly reduce the I-domain binding activity to soluble duanyu1648 and the alanine substitutions of basic amino acids on the flat surface of the V-domain prevent the V-domain binding to αX I-domain. In conclusion, the main mechanism of αX I-domain binding to duanyu1648 is a charge interaction, in which the acidic moieties of αX I-domains, including E244, and D249, recognize the basic residues on the duanyu1648 V-domain encompassing K39, K43, K44, R104, and K107.

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