Title : Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.

Pub. Date : 2013 Jul 15

PMID : 23677799






4 Functional Relationships(s)
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Protein Name
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1 Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines. Disulfides claudin 2 Canis lupus familiaris
2 Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2. Disulfides claudin 2 Canis lupus familiaris
3 Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2. Disulfides claudin 2 Canis lupus familiaris
4 We conclude that the disulfide bond between the conserved extracellular cysteines in claudin-2 is necessary for pore formation, probably by stabilizing the ECL1 fold, but is not required for correct protein trafficking. Disulfides claudin 2 Canis lupus familiaris