PDBsum entry 5ao6

Endocytosis

PDB id: 5ao6

Contents

Protein chains

430 a.a.

PDB id:

5ao6

Name:

Endocytosis

Title:

Endo180 d1-4, trigonal form

Structure:

C-type mannose receptor 2. Chain: a, b. Fragment: domains 1-4, unp residues 35-511. Synonym: c-type lectin domain family 13 member e, endocytic receptor 180, macrophage mannose receptor 2, urokinase-type plasminogen activator receptor-associated protein, upar-associated protein, urokinase receptor-associated protein, c-type lectin domain family 13 member e, endocytic receptor 180, macrophage mannose receptor 2, urokinase-type plasminogen activator receptor-associated protein,

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606.

Resolution:

3.36Å R-factor: 0.225 R-free: 0.306

Authors:

P.Paracuellos,D.C.Briggs,F.Carafoli,T.Loncar,E.Hohenester

Key ref:

P.Paracuellos et al. (2015). Insights into Collagen Uptake by C-type Mannose Receptors from the Crystal Structure of Endo180 Domains 1-4. Structure, 23, 2133-2142. PubMed id: 26481812 DOI: 10.1016/j.str.2015.09.004

Date:

09-Sep-15 Release date: 28-Oct-15

Protein chains

Q9UBG0  (MRC2_HUMAN) -  C-type mannose receptor 2 from Homo sapiens

Seq: 1479 a.a.

Struc: 430 a.a.

DOI no: 10.1016/j.str.2015.09.004

Structure 23:2133-2142 (2015)

PubMed id: 26481812

Insights into Collagen Uptake by C-type Mannose Receptors from the Crystal Structure of Endo180 Domains 1-4.

P.Paracuellos, D.C.Briggs, F.Carafoli, T.Lončar, E.Hohenester.

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.