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PDBsum entry 5ao6
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References listed in PDB file
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Key reference
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Title
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Insights into collagen uptake by c-Type mannose receptors from the crystal structure of endo180 domains 1-4.
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Authors
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P.Paracuellos,
D.C.Briggs,
F.Carafoli,
T.Lončar,
E.Hohenester.
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Ref.
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Structure, 2015,
23,
2133-2142.
[DOI no: ]
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PubMed id
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Abstract
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The C-type mannose receptor and its homolog Endo180 (or uPARAP, for urokinase
plasminogen activator receptor-associated protein) mediate the endocytic uptake
of collagen by macrophages and fibroblasts. This process is required for normal
tissue remodeling, but also facilitates the growth and dissemination of tumors.
We have determined the crystal structure at 2.5 Å resolution of the N-terminal
region of Endo180, consisting of a ricin-like domain, a fibronectin type II
(FN2) domain, and two C-type lectin (CTL) domains. The L-shaped arrangement of
these domains creates a shallow trench spanning the FN2 and CTL1 domains, which
was shown by mutagenesis to bind triple-helical and denatured collagen.
Small-angle X-ray scattering showed that the L-shaped structure is maintained in
solution at neutral and acidic pH, irrespective of calcium ion loading. Collagen
binding was equally unaffected by acidic pH, suggesting that collagen release in
endosomes is not regulated by changes within the Endo180 N-terminal region.
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