About: Autonomous Tetramerization Domains in the Glycan-binding Receptors DC-SIGN and DC-SIGNR

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About: Autonomous Tetramerization Domains in the Glycan-binding Receptors DC-SIGN and DC-SIGNR Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Autonomous Tetramerization Domains in the Glycan-binding Receptors DC-SIGN and DC-SIGNR
Creator	Drickamer, Kurt Yang, Chunxuan Oldring, Asa Powlesland, Alex Taylor⁎, Maureen Tso, Cynthia Yu, Quan
Source	Elsevier; Medline; PMC
abstract	Multivalent binding of glycans on pathogens and on mammalian cells by the receptors DC-SIGN (CD209) and DC-SIGNR (L-SIGN, CD299) is dependent on correct disposition of the C-type carbohydrate-recognition domains projected at the C-terminal ends of necks at the cell surface. In the work reported here, neck domains of DC-SIGN and DC-SIGNR expressed in isolation are shown to form tetramers in the absence of the CRDs. Stability analysis indicates that interactions between the neck domains account fully for the stability of the tetrameric extracellular portions of the receptors. The neck domains are approximately 40% α-helical based on circular dichroism analysis. However, in contrast to other glycan-binding receptors in which fully helical neck regions are intimately associated with C-terminal C-type CRDs, the neck domains in DC-SIGN and DC-SIGNR act as autonomous tetramerization domains and the neck domains and CRDs are organized independently. Neck domains from polymorphic forms of DC-SIGNR that lack some of the repeat sequences show modestly reduced stability, but differences near the C-terminal end of the neck domains lead to significantly enhanced stability of DC-SIGNR tetramers compared to DC-SIGN.
has issue date	2009-04-17(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2009.02.046
bibo:pmid	19249311
has license	cc-by
sha1sum (hex)	e8c8602036bc1b4f55f283f6920abadde465a1d1
schema:url	https://doi.org/10.1016/j.jmb.2009.02.046
resource representing a document's title	Autonomous Tetramerization Domains in the Glycan-binding Receptors DC-SIGN and DC-SIGNR
has PubMed Central identifier	PMC2680971
has PubMed identifier	19249311
schema:publication	J Mol Biol
resource representing a document's body	covid:e8c8602036bc1b4f55f283f6920abadde465a1d1#body_text
is schema:about of	named entity 'AUTONOMOUS' named entity 'surface' named entity 'Stability' named entity 'necks' named entity 'domains' named entity 'glycans' named entity 'Domains' named entity 'BASED' named entity 'CRDS' named entity 'GLYCANS' named entity 'ASSOCIATED WITH' named entity 'DEPENDENT' named entity 'CORRECT' named entity 'NECKS' named entity 'ENHANCED' named entity 'TYPE' named entity 'CD299' named entity 'NECK' named entity 'PROJECTED' named entity 'LACK' named entity 'TO FORM' named entity 'STABILITY' named entity 'DC-SIGNR' named entity 'C-TERMINAL' named entity 'GLYCAN' named entity 'HELICAL' named entity 'FORMS' named entity 'RECOGNITION' named entity 'MAMMALIAN' named entity 'HERE' named entity 'INTERACTIONS' named entity 'WORK' named entity 'APPROXIMATELY' named entity 'END' named entity 'REPEAT SEQUENCES' named entity 'CIRCULAR DICHROISM' named entity 'CONTRAST' named entity 'RECEPTORS' named entity 'DC-SIGN' named entity '40%' named entity 'AUTONOMOUS' named entity 'DISPOSITION' named entity 'RECEPTORS' named entity 'BINDING' named entity 'GLYCAN' named entity 'EXPRESSED' named entity 'BUT' named entity 'POLYMORPHIC' named entity 'CARBOHYDRATE' named entity 'EXTRACELLULAR' named entity 'REDUCED' named entity 'ACT' named entity 'ISOLATION' named entity 'ENDS' named entity 'BINDING' named entity 'REGIONS' named entity 'COMPARED' named entity 'DC-SIGN' named entity 'SIGN' named entity 'ACCOUNT' named entity 'CELLS' named entity 'PATHOGENS' named entity 'REPORTED' named entity 'LEAD' named entity 'DC-SIGNR' named entity 'FULLY' named entity 'ANALYSIS' named entity 'ABSENCE OF' named entity 'CELL SURFACE' named entity 'THE NECK' named entity 'ORGANIZED' named entity 'NEAR' covid:arg/e8c8602036bc1b4f55f283f6920abadde465a1d1 named entity 'dependent' named entity 'domains'

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