About: Chicken GRIFIN: Structural characterization in crystals and in solution

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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	Chicken GRIFIN: Structural characterization in crystals and in solution
Creator	Gabius, Hans-Joachim Kaltner, Herbert Romero, Antonio Gilles, Ulrich Lindner, Ingo Ludwig, Anna-Kristin Reusch, Dietmar Sehad, Celia Caballero, Gabriel Roy, Ren Ruiz, Federico Shiao, Tze
Source	Elsevier; Medline; PMC
abstract	Abstract Despite its natural abundance in lenses of vertebrates the physiological function(s) of the galectin-related inter-fiber protein (GRIFIN) is (are) still unclear. The same holds true for the significance of the unique interspecies (fish/birds vs mammals) variability in the capacity to bind lactose. In solution, ultracentrifugation and small angle X-ray scattering (at concentrations up to 9 mg/mL) characterize the protein as compact and stable homodimer without evidence for aggregation. The crystal structure of chicken (C-)GRIFIN at seven pH values from 4.2 to 8.5 is reported, revealing compelling stability. Binding of lactose despite the Arg71Val deviation from the sequence signature of galectins matched the otherwise canonical contact pattern with thermodynamics of an enthalpically driven process. Upon lactose accommodation, the side chain of Arg50 is shifted for hydrogen bonding to the 3-hydroxyl of glucose. No evidence for a further ligand-dependent structural alteration was obtained in solution by measuring hydrogen/deuterium exchange mass spectrometrically in peptic fingerprints. The introduction of the Asn48Lys mutation, characteristic for mammalian GRIFINs that have lost lectin activity, lets labeled C-GRIFIN maintain capacity to stain tissue sections. Binding is no longer inhibitable by lactose, as seen for the wild-type protein. These results establish the basis for detailed structure-activity considerations and are a step to complete the structural description of all seven members of the galectin network in chicken.
has issue date	2018-03-31(xsd:dateTime)
bibo:doi	10.1016/j.biochi.2017.12.003
bibo:pmid	29248541
has license	els-covid
sha1sum (hex)	1141c480cc6ab01d00721ee772ea39d4b74eb615
schema:url	https://doi.org/10.1016/j.biochi.2017.12.003
resource representing a document's title	Chicken GRIFIN: Structural characterization in crystals and in solution
has PubMed Central identifier	PMC7115793
has PubMed identifier	29248541
schema:publication	Biochimie
resource representing a document's body	covid:1141c480cc6ab01d00721ee772ea39d4b74eb615#body_text
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