High impact information on TXNDC10

• Here we describe the identification and characterization of a novel member of the human PDI family, TMX3 (thioredoxin-related transmembrane protein 3) [1].
• Circular dichroism spectroscopy of the recombinantly expressed luminal domain of TMX3 showed features typical of a properly folded protein of the alpha/beta type [1].
• Interestingly, TMX3 showed oxidase activity, and in human tissue-culture cells the protein was found partially in the oxidized form, potentially suggesting a function of the protein as a dithiol oxidase [1].
• The partitioning of TMX-3 into membranes followed complex kinetics, induced helicity, and shifted the histidine pK(a) from 6.8 to approximately 6 [2].
• TMX-3 has two important structural features: a proline residue in the hydrophobic core that discourages the formation of highly helical aggregates in solution and two histidine residues that allow control of membrane and solution interactions by means of pH changes [2].

Associations of TXNDC10 with chemical compounds

• These results show that histidine titration is likely to be important in the pH-dependent refolding of toxins on membrane interfaces and that the most favored state of TMX-3 under any conditions is the IF folded state, which emphasizes the importance of such states in the spontaneous refolding and insertion of diphtheria and other membrane toxins [2].

Analytical, diagnostic and therapeutic context of TXNDC10

• Endogenous TMX3 contains endoglycosidase H-sensitive glycans, localizes to the ER by immunofluorescence microscopy, and is present in the membrane fraction after alkaline extraction of the ER luminal content [1].

References