Crystal structure of the C‐terminal conserved domain of human GRP, a galectin‐related protein, reveals a function mode different from those of galectins

Zhou, Dongwen; Ge, Honghua; Sun, Jianyuan; Gao, Yongxiang; Teng, Maikun; Niu, Liwen

doi:10.1002/prot.22003

Cited by 21 publications

(23 citation statements)

References 43 publications

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“…34 Recently, the structure of the C-terminal conserved domain of human GRP (hGRPC) was resolved in its free form, and consistent with prior reports, no apparent lectin activity was identified within this protein structure. 15 …”

Section: Structural Aspects Of Galectin–glycan Interactionsmentioning

confidence: 99%

When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again

et al. 2011

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In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings.

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Section: Structural Aspects Of Galectin–glycan Interactionsmentioning

confidence: 99%

When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again

et al. 2011

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“…When applying this concept to the adhesion/ growth-regulatory galectins, to bring the status of knowledge for the galectin-related protein (GRP), an integral part of the phylogeny of this class of lectins [3,4], to the same level as already attained for canonical proteins was an obvious necessity. In this case, the indications for an exceptionally high level of sequence conservation among vertebrates [3], the loss of binding to the common ligand lactose for human GRP [5,6] and the general status of the five canonical chicken galectins (CGs) as model suited for comprehensive network analysis of general relevance [7] had prompted detailed biochemical characterization of chicken GRP (C-GRP) [8]. Except for the occurrence of C-GRP-specific mRNA in bursal lymphocytes [3], no information on expression of this gene was available for this sixth member of the galectin family in chicken or for any other vertebrate.…”

Section: Introductionmentioning

confidence: 95%

Galectin-related protein: An integral member of the network of chicken galectins

Kaltner

Caballero

Sinowatz

et al. 2016

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…In solution, C-GRP-C, like human GRP-C, is monomeric (50,52,53) and not active as haemagglutinin (50). Interestingly, rat galectin-5 that shares presence of an N-terminal extension and monomer status in solution is a weak haemagglutinin (57,58).…”

Section: Structure Of Grpmentioning

confidence: 99%

“…Furthermore, purification of GRP-C had to include a tagging approach, because these GRPs indeed lacked binding to lactose-bearing beads commonly used for affinity chromatography. Crystals of human and chicken GRP-C diffracted X-rays to a resolution of 2.0 (human) and 1.55 (chicken) (50)(51)(52)(53). As shown for chicken GRP-C (C-GRP-C) in Thus, the central positions for 'reading' the axial 4-hydroxyl group of galactose are lost (14).…”

Section: Structure Of Grpmentioning

confidence: 99%

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 2. Galectin-Related Protein (GRP)

Manning¹,

Caballero²,

Ruiz

et al. 2018

TIGG

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Galectin-related protein (GRP) is present in vertebrates. Sequence comparisons between GRPs from diverse species reveal an unusually high degree of similarity indicative of a strong positive selection. In solution, human and chicken GRPs are monomers irrespective of the presence of the 36-amino-acid-long extension of the core structure at the N-terminus. They are devoid of ability to bind lactose due to severe deviations from the respective sequence signature. Crystallography disclosed distortion of the binding-site architecture that precludes accommodation of lactose. The recent characterization of expression of chicken GRP (C-GRP) enables complete galectin network analysis in this organism. When tested in a panel of developing and adult organs, C-GRP presence was detected in bursa of Fabricius. Its epithelium and vessels as well as bursal B cells are positive in immunohistochemistry. In the B lymphocytes, C-GRP was predominantly cytoplasmic, whereas the chicken tandem-repeat-type galectin, the second member of the galectin family expressed in these cells, was detected at the surface. Binding of labeled C-GRP to cells and sections was blocked by heparin. These data illustrate disparities in expression and ligand profiles within the galectin family and hereby stimulate interest to perform respective mapping for mammalian GRPs as step to define its physiological function(s). A. IntroductionThe prominent positioning of glycans on cell surfaces is ideal for major functions in cell sociology, what has provoked curiosity and the interest to understand why they appear to be a molecular fingerprint (1). In terms of structural variability, a wide array of enzymes is responsible for ensuring that glycans realize their unsurpassed capacity to store biological information in a minimum of space (2-13). Remarkably, the study of glycan structures in relation to phylogenesis revealed a separation into distinct profiles, e.g. yeast, worm, insect or mammalian N-glycosylation with an emergence of intricate (complex-type) branch-end tailoring in vertebrates (14-16). Since the termini of glycan chains are readily accessible for molecular recognition by receptors (lectins), the ensuing functional pairing has become an integral part of our view on the flow of biological information (17), directing attention to studying these 'readers' of sugar-encoded 'messages.' Indeed, protein folds with sites to accommodate glycans occur frequently in Nature and have been delineated as versatile platforms for generating a wide variety of lectins (18)(19)(20)(21)(22)(23)(24). As their thorough analysis on the level of genes and crystal structures attests, an ancestral motif is the starting point for generating up to multiple homologous proteins during the course of evolution, a process establishing diversity in the families of lectins (18,23,(25)(26)(27)(28)(29)(30). Among them, the ga(lactose-binding)lectins that share the β-sandwich fold provide an instructive example for forming a network of β-galactosidespecific receptors (29,(31)(32)(3...

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Crystal structure of the C‐terminal conserved domain of human GRP, a galectin‐related protein, reveals a function mode different from those of galectins

Cited by 21 publications

References 43 publications

When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again

When Galectins Recognize Glycans: From Biochemistry to Physiology and Back Again

Galectin-related protein: An integral member of the network of chicken galectins

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 2. <i>G</i>alectin-<i>R</i>elated <i>P</i>rotein (GRP)

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