dc.contributor.author | East, L | |
dc.contributor.author | Rushton, S | |
dc.contributor.author | Taylor, ME | |
dc.contributor.author | Isacke, CM | |
dc.date.accessioned | 2018-07-31T14:35:01Z | |
dc.date.issued | 2002-12-27 | |
dc.identifier.citation | The Journal of biological chemistry, 2002, 277 (52), pp. 50469 - 50475 | |
dc.identifier.issn | 0021-9258 | |
dc.identifier.uri | https://repository.icr.ac.uk/handle/internal/2237 | |
dc.identifier.eissn | 1083-351X | |
dc.identifier.doi | 10.1074/jbc.m208985200 | |
dc.description.abstract | Members of the mannose receptor family, the mannose receptor, the phospholipase A(2) receptor, DEC-205, and Endo180, contain multiple C-type lectin-like domains (CTLDs) within a single polypeptide. In addition, at their N termini, all four family members contain a cysteine-rich domain similar to the R-type carbohydrate recognition domains of ricin. However, despite the common presence of multiple lectin-like domains, these four endocytic receptors have divergent ligand binding activities, and it is clear that the majority of these domains do not bind sugars. Here the functions of the lectin-like domains of the most recently discovered family member, Endo180, have been investigated. Endo180 is shown to bind in a Ca(2+)-dependent manner to mannose, fucose, and N-acetylglucosamine but not to galactose. This activity is mediated by one of the eight CTLDs, CTLD2. Competition assays indicate that the monosaccharide binding specificity of Endo180 CTLD2 is similar to that of mannose receptor CTLD4. However, additional experiments indicate that, unlike the cysteine-rich domain of the mannose receptor, the cysteine-rich domain of Endo180 does not bind sulfated sugars. Thus, although Endo180 and the mannose receptor are now both known to be mannose binding lectins, each receptor is likely to have a distinct set of glycoprotein ligands in vivo. | |
dc.format | Print-Electronic | |
dc.format.extent | 50469 - 50475 | |
dc.language | eng | |
dc.language.iso | eng | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.subject | Humans | |
dc.subject | Calcium | |
dc.subject | Monosaccharides | |
dc.subject | Peptide Fragments | |
dc.subject | Membrane Glycoproteins | |
dc.subject | Lectins | |
dc.subject | Lectins, C-Type | |
dc.subject | Mannose-Binding Lectins | |
dc.subject | Receptors, Cell Surface | |
dc.subject | Receptors, Mitogen | |
dc.subject | Recombinant Proteins | |
dc.subject | DNA Primers | |
dc.subject | Restriction Mapping | |
dc.subject | Cloning, Molecular | |
dc.subject | Binding Sites | |
dc.subject | Amino Acid Sequence | |
dc.subject | Base Sequence | |
dc.subject | Substrate Specificity | |
dc.subject | Kinetics | |
dc.subject | Molecular Sequence Data | |
dc.title | Characterization of sugar binding by the mannose receptor family member, Endo180. | |
dc.type | Journal Article | |
rioxxterms.versionofrecord | 10.1074/jbc.m208985200 | |
rioxxterms.licenseref.startdate | 2002-12 | |
rioxxterms.type | Journal Article/Review | |
dc.relation.isPartOf | The Journal of biological chemistry | |
pubs.issue | 52 | |
pubs.notes | Not known | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology | |
pubs.organisational-group | /ICR | |
pubs.organisational-group | /ICR/Primary Group | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research | |
pubs.organisational-group | /ICR/Primary Group/ICR Divisions/Breast Cancer Research/Molecular Cell Biology | |
pubs.publication-status | Published | |
pubs.volume | 277 | |
pubs.embargo.terms | Not known | |
icr.researchteam | Molecular Cell Biology | |
dc.contributor.icrauthor | Isacke, Clare | |