https://sivelestatinhibitor.co....m/fine-mapping-in-th
The two mutations at the EKE282 position of the BTN2A1 protein's juxtamembrane region exhibited no impact on the protein's function. Unlike other mutations, single-point changes (L318G and L325G) proximate to the BTN2A1 B302 domain suppressed the phospho-Ag response. Size exclusion chromatography and NMR spectroscopy experiments underscored that the isolated BTN2A1 B302 domain, while lacking its extracellular and transmembrane components, maintains a homodimeric state.
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