Title : Probing the structural flexibility of the human copper metallochaperone Atox1 dimer and its interaction with the CTR1 c-terminal domain.

Pub. Date : 2014 Jun 5

PMID : 24837030






2 Functional Relationships(s)
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1 This study also shows that the last three amino acids of the CTR1 c-terminal domain, HCH, are important for maintaining the crystal structure of the Atox1, allowing less structural flexibility and improved thermal stability of Atox1. alpha-hexachlorocyclohexane antioxidant 1 copper chaperone Homo sapiens
2 This study also shows that the last three amino acids of the CTR1 c-terminal domain, HCH, are important for maintaining the crystal structure of the Atox1, allowing less structural flexibility and improved thermal stability of Atox1. alpha-hexachlorocyclohexane antioxidant 1 copper chaperone Homo sapiens