Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain
Skipwith C, Stayrook S, Rottensteiner H, Scheiflinger F, Zheng X. Crystal Structure of a Proteolytic Fragment of ADAMTS13 Reveals Alternative Disulfide Pairings in the Cysteine-Rich Domain. Blood 2012, 120: 3363. DOI: 10.1182/blood.v120.21.3363.3363.Peer-Reviewed Original ResearchIntermolecular disulfide bondsSpacer domainExosite interactionsProteolytic fragmentsDisulfide bondsNon-catalytic domainStably transfected Chinese hamster ovary cellsCysteine-rich domainChinese hamster ovary cellsDisulfide pairing patternADAMTS13 spacer domainHamster ovary cellsCys-richCrystallization screeningCysteine residuesDiffracting crystalsVon Willebrand factorX-ray diffractionFree cysteine residuesDisulfide bond pairingsDisulfide pairingPairing patternsCA domainOvary cellsResidues