Extended and bent conformations of the mannose receptor family

@article{Llorca2007ExtendedAB,
  title={Extended and bent conformations of the mannose receptor family},
  author={Oscar Llorca},
  journal={Cellular and Molecular Life Sciences},
  year={2007},
  volume={65},
  pages={1302-1310}
}
  • O. Llorca
  • Published 12 January 2008
  • Biology, Medicine
  • Cellular and Molecular Life Sciences
Abstract.In mammals, the mannose receptor family consists of four members, Endo180, DEC-205, phospholipase A2 receptor and the mannose receptor. The extracellular domains of all these receptors contain a similar arrangement of domains in which an Nterminal cysteine-rich domain is followed by a single fibronectin type II domain and eight or ten C-type lectin-like domains. This review focuses on the threedimensional structure of the receptors in the mannose receptor family and its functional… Expand
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TLDR
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R-Type Lectins
TLDR
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From lectin structure to functional glycomics: principles of the sugar code.
TLDR
The strategic combination of methods to monitor distinct aspects of the lectin-glycan interplay offers a promising perspective to answer the central question of how the exquisite target specificity of endogenous lectins for certain cellular glycans can be explained. Expand
Identification of the ovine mannose receptor and its possible role in Visna/Maedi virus infection
TLDR
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TLDR
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References

SHOWING 1-10 OF 76 REFERENCES
The mannose receptor family.
The mannose receptor family comprises four glycoproteins each of which is a type I transmembrane receptor with an N-terminal cysteine-rich domain, a single fibronectin type II (FNII) domain and eightExpand
An Extended Conformation of the Macrophage Mannose Receptor*
TLDR
Hydrodynamic coefficients predicted for modeled receptor conformations are consistent with an extended conformation with close contacts between three pairs of CRDs. Expand
Structural Model for the Mannose Receptor Family Uncovered by Electron Microscopy of Endo180 and the Mannose Receptor*
TLDR
It is found that both receptors display distinct three-dimensional structures, which are, however, conceptually very similar: a bent and compact conformation built upon interactions of the CysR domain and the lone functional CTLD. Expand
Characterization of Sugar Binding by the Mannose Receptor Family Member, Endo180*
TLDR
Endo180 is shown to bind in a Ca2+-dependent manner to mannose, fucose, and N-acetylglucosamine but not to galactose and competition assays indicate that the monosaccharide binding specificity of Endo180 CTLD2 is similar to that of mannoses receptor CTLD4. Expand
The C-type Lectin Receptor Endo180 Displays Internalization and Recycling Properties Distinct from Other Members of the Mannose Receptor Family*
TLDR
Findings demonstrate that despite an overall structural similarity, members of this receptor family employ distinct trafficking mechanisms that may reflect important differences in their physiological functions. Expand
Structure of a C-type Carbohydrate Recognition Domain from the Macrophage Mannose Receptor*
TLDR
The crystal structure of CRD-4 suggests a mechanism for endosomal ligand release in which the auxiliary calcium site serves as a pH sensor and the principal site known to mediate carbohydrate binding in other C-type lectins is occupied. Expand
Contribution to ligand binding by multiple carbohydrate-recognition domains in the macrophage mannose receptor.
The extracellular portion of the macrophage mannose receptor is composed of several cysteine-rich domains, including a fibronectin type II repeat and eight segments related in sequence toExpand
Crystal Structure of the Cysteine-Rich Domain of Mannose Receptor Complexed with a Sulfated Carbohydrate Ligand
TLDR
To elucidate the mechanism of sulfated carbohydrate recognition, crystal structures of Cys-MR alone and complexed with 4-sulfated-N-acetylgalactosamine are determined and used to rationalize the carbohydrate binding specificities of CYS-MR and compare the recognition properties of Ccy-MR with other β-trefoil proteins. Expand
Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing.
TLDR
The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two Holmium ions. Expand
Collagen binding by the mannose receptor mediated through the fibronectin type II domain.
TLDR
This work has shown that the mannose receptor can also bind collagen and that the fibronectin type II domain mediates this activity, and suggested additional roles for this multifunctional receptor in mediating collagen clearance or cell-matrix adhesion. Expand
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