5E4K
Structure of ligand binding region of uPARAP at pH 7.4
Summary for 5E4K
| Entry DOI | 10.2210/pdb5e4k/pdb |
| Related | 5E4L |
| Descriptor | C-type mannose receptor 2, CALCIUM ION, SODIUM ION, ... (7 entities in total) |
| Functional Keywords | endocytic collagen receptor, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Cellular location | Membrane; Single-pass type I membrane protein: Q9UBG0 |
| Total number of polymer chains | 1 |
| Total formula weight | 57064.17 |
| Authors | |
| Primary citation | Yuan, C.,Jurgensen, H.J.,Engelholm, L.H.,Li, R.,Liu, M.,Jiang, L.,Luo, Z.,Behrendt, N.,Huang, M. Crystal structures of the ligand-binding region of uPARAP: effect of calcium ion binding Biochem.J., 473:2359-2368, 2016 Cited by PubMed Abstract: The proteins of the mannose receptor (MR) family share a common domain organization and have a broad range of biological functions. Urokinase plasminogen activator receptor-associated protein (uPARAP) (or Endo180) is a member of this family and plays an important role in extracellular matrix remodelling through interaction with its ligands, including collagens and urokinase plasminogen activator receptor (uPAR). We report the crystal structures of the first four domains of uPARAP (also named the ligand-binding region, LBR) at pH 7.4 in Ca(2+)-bound and Ca(2+)-free forms. The first domain (cysteine-rich or CysR domain) folds into a new and unique conformation different from the β-trefoil fold of typical CysR domains. The so-called long loop regions (LLRs) of the C-type lectin-like domain (CTLD) 1 and 2 (the third and fourth domain) mediate the direct contacts between these domains. These LLRs undergo a Ca(2+)-dependent conformational change, and this is likely to be the key structural determinant affecting the overall conformation of uPARAP. Our results provide a molecular mechanism to support the structural flexibility of uPARAP, and shed light on the structural flexibility of other members of the MR family. PubMed: 27247422DOI: 10.1042/BCJ20160276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.58 Å) |
Structure validation
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