{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,15]],"date-time":"2026-07-15T21:54:29Z","timestamp":1784152469824,"version":"3.55.0"},"reference-count":34,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2005,3,1]]},"abstract":"<jats:p>Mammalian sulphatases (EC 3.1.6) are a family of enzymes that have a high degree of similarity in amino acid sequence, structure and catalytic mechanism. IDS (iduronate-2-sulphatase; EC\u00a03.1.6.13) is a lysosomal exo-sulphatase that belongs to this protein family and is involved in the degradation of the glycosaminoglycans heparan sulphate and dermatan sulphate. An IDS deficiency causes the lysosomal storage disorder MPS II (mucopolysaccharidosis type II). To examine the structural alterations in heat-denatured and mutant IDS, a panel of four monoclonal antibodies was raised to the denatured protein and used as probes of protein conformation. The linear sequence epitope reactivity of a polyclonal antibody raised against the native protein and the monoclonal antibodies were defined and mapped to distinct regions on the IDS protein. The antigenicity of native IDS was higher in regions without glycosylation, but reactivity was not restricted to protein surface epitopes. One monoclonal epitope was relatively surface accessible and in close proximity to an N-linked glycosylation site, while three others required additional thermal energy to expose the epitopes. The monoclonal antibodies demonstrated the capacity to differentiate progressive structural changes in IDS and could be used to characterize the severity of MPS type II in patients based on variable denatured microstates.<\/jats:p>","DOI":"10.1042\/bj20040739","type":"journal-article","created":{"date-parts":[[2005,2,22]],"date-time":"2005-02-22T12:53:44Z","timestamp":1109076824000},"page":"395-400","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":17,"title":["Analysis of normal and mutant iduronate-2-sulphatase conformation"],"prefix":"10.1042","volume":"386","author":[{"given":"Emma","family":"PARKINSON-LAWRENCE","sequence":"first","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Genetic Medicine, Women's and Children's Hospital, 72 King William Rd, North Adelaide, South Australia 5006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher","family":"TURNER","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Genetic Medicine, Women's and Children's Hospital, 72 King William Rd, North Adelaide, South Australia 5006, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"HOPWOOD","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Genetic Medicine, Women's and Children's Hospital, 72 King William Rd, North Adelaide, South Australia 5006, Australia"},{"name":"Department of Paediatrics, University of Adelaide, Adelaide, South Australia 5005, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doug","family":"BROOKS","sequence":"additional","affiliation":[{"name":"Lysosomal Diseases Research Unit, Department of Genetic Medicine, Women's and Children's Hospital, 72 King William Rd, North Adelaide, South Australia 5006, Australia"},{"name":"Department of Paediatrics, University of Adelaide, Adelaide, South Australia 5005, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2005,2,22]]},"reference":[{"key":"2021112217113962000_B1","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/S0969-2126(01)00609-8","article-title":"1.3 \u00c5 structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family","volume":"9","author":"Boltes","year":"2001","journal-title":"Structure"},{"key":"2021112217113962000_B2","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0969-2126(97)00185-8","article-title":"Structure of a human lysosomal sulfatase","volume":"5","author":"Bond","year":"1997","journal-title":"Structure"},{"key":"2021112217113962000_B3","doi-asserted-by":"crossref","first-page":"3654","DOI":"10.1021\/bi9714924","article-title":"Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis","volume":"37","author":"Lukatela","year":"1998","journal-title":"Biochemistry"},{"key":"2021112217113962000_B4","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1006\/jmbi.2000.4297","article-title":"Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis","volume":"305","author":"von\u00a0Bulow","year":"2001","journal-title":"J. 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