5AO6

Endo180 D1-4, trigonal form

Summary for 5AO6

• Entry DOI: 10.2210/pdb5ao6/pdb
• Related: 5AO5
• Descriptor: C-TYPE MANNOSE RECEPTOR 2 (1 entity in total)
• Functional Keywords: endocytosis, endocytic receptor, fibronectin type ii domain, c-type lectin domain, collagen, gelatin
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 111269.18

Authors

Paracuellos, P.,Briggs, D.C.,Carafoli, F.,Loncar, T.,Hohenester, E. (deposition date: 2015-09-09, release date: 2015-10-28, Last modification date: 2024-11-20)

Primary citation

Paracuellos, P.,Briggs, D.C.,Carafoli, F.,Loncar, T.,Hohenester, E.
Insights Into Collagen Uptake by C-Type Mannose Receptors from the Crystal Structure of Endo180 Domains 1-4.
Structure, 23:2133-, 2015

PubMed Abstract: 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.

PubMed: 26481812
DOI: 10.1016/J.STR.2015.09.004

Experimental method

X-RAY DIFFRACTION (3.36 Å)