Počet záznamů: 1

Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition

  1. 1.
    0359104 - UMG-J 2011 RIV DK eng J - Článek v odborném periodiku
    Krejčiříková, Veronika - Pachl, Petr - Fábry, Milan - Malý, Petr - Řezáčová, Pavlína - Brynda, Jiří
    Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition.
    [Struktura N-terminální domény myšího galectinu-4 odhaluje mechanismus rozpoznávání oligosacharidů.]
    Acta Crystallographica Section D-Biological Crystallography. Roč. 67, Pt3 (2011), 204-211 ISSN 0907-4449
    Grant CEP: GA ČR GA203/09/0820; GA ČR GA304/03/0090; GA ČR GA301/07/0600
    Výzkumný záměr: CEZ:AV0Z50520514; CEZ:AV0Z50520701; CEZ:AV0Z40550506
    Klíčová slova: S-type lectins * carbohydrate binding * molecular recognition
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 12.619, rok: 2011

    Galectin-4, a member of the tandem-repeat subfamily of galectins, participates in cell-membrane interactions and plays an important role in cell adhesion and modulation of immunity and malignity. The oligosaccharide specificity of the mouse galectin-4 carbohydrate-recognition domains (CRDs) has been reported previously. In this work, the structure and binding properties of the N-terminal domain CRD1 were further investigated and the crystal structure of CRD1 in complex with lactose was determined at 2.1 Ǻ resolution. The lactose-binding affinity was characterized by fluorescence measurements and two lactose-binding sites were identified: a high-affinity site with a Kd value in the micromolar range (Kd1 = 600 ± 70 mM) and a low-affinity site with Kd2 = 28 ± 10 mM.
    Trvalý link: http://hdl.handle.net/11104/0006423
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