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dc.contributor.authorDelker, Silvia L.en
dc.contributor.authorWest, Anthony P.en
dc.contributor.authorMcDermott, Lindsay C.en
dc.contributor.authorKennedy, Malcolm W.en
dc.contributor.authorBjorkman, Pamela J.en
dc.date.accessioned2018-04-27T10:24:01Z
dc.date.available2018-04-27T10:24:01Z
dc.date.issued2004-05-19
dc.identifier.citationDelker SL, West AP, McDermott L, Kennedy MW, Bjorkman PJ (2004) 'Crystallographic studies of ligand binding by Zn-alpha(2)-glycoprotein', Journal of Structural Biology, 148 (2), pp.205-213.en
dc.identifier.issn1047-8477
dc.identifier.pmid15477100
dc.identifier.doi10.1016/j.jsb.2004.04.009
dc.identifier.urihttp://hdl.handle.net/10547/622681
dc.description.abstractZn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. The previously reported 2.8 A crystal structure of ZAG isolated from human serum demonstrated the structural similarity between ZAG and class I major histocompatibility complex (MHC) molecules and revealed a non-peptidic ligand in the ZAG counterpart of the MHC peptide-binding groove. Here we present crystallographic studies to explore further the nature of the non-peptidic ligand in the ZAG groove. Comparison of the structures of several forms of recombinant ZAG, including a 1.95 A structure derived from ZAG expressed in insect cells, suggests that the non-peptidic ligand in the current structures and in the structure of serum ZAG is a polyethylene glycol (PEG), which is present in the crystallization conditions used. Further support for PEG binding in the ZAG groove is provided by the finding that PEG displaces a fluorophore-tagged fatty acid from the ZAG binding site. From these results we hypothesize that our purified forms of ZAG do not contain a bound endogenous ligand, but that the ZAG groove is capable of binding hydrophobic molecules, which may relate to its function.
dc.language.isoenen
dc.publisherElsevieren
dc.relation.urlhttps://www.sciencedirect.com/science/article/pii/S1047847704001029en
dc.rightsGreen - can archive pre-print and post-print or publisher's version/PDF
dc.subjectobesityen
dc.subjectn-3 polyunsaturated fatty acidsen
dc.subjectC700 Molecular Biology, Biophysics and Biochemistryen
dc.titleCrystallographic studies of ligand binding by Zn-alpha(2)-glycoproteinen
dc.typeArticleen
dc.contributor.departmentCalifornia Institute of Technologyen
dc.contributor.departmentUniversity of Glasgowen
dc.identifier.journalJournal of Structural Biologyen
dc.date.updated2018-04-27T09:56:41Z
html.description.abstractZn-alpha2-glycoprotein (ZAG) is a 41 kDa soluble protein that is present in most bodily fluids. The previously reported 2.8 A crystal structure of ZAG isolated from human serum demonstrated the structural similarity between ZAG and class I major histocompatibility complex (MHC) molecules and revealed a non-peptidic ligand in the ZAG counterpart of the MHC peptide-binding groove. Here we present crystallographic studies to explore further the nature of the non-peptidic ligand in the ZAG groove. Comparison of the structures of several forms of recombinant ZAG, including a 1.95 A structure derived from ZAG expressed in insect cells, suggests that the non-peptidic ligand in the current structures and in the structure of serum ZAG is a polyethylene glycol (PEG), which is present in the crystallization conditions used. Further support for PEG binding in the ZAG groove is provided by the finding that PEG displaces a fluorophore-tagged fatty acid from the ZAG binding site. From these results we hypothesize that our purified forms of ZAG do not contain a bound endogenous ligand, but that the ZAG groove is capable of binding hydrophobic molecules, which may relate to its function.


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