3ZHG
Crystallographic structure of the native mouse SIGN-R1 CRD domain
Summary for 3ZHG
| Entry DOI | 10.2210/pdb3zhg/pdb |
| Related | 3ZG5 3ZH3 3ZH4 |
| Descriptor | CD209 ANTIGEN-LIKE PROTEIN B, SULFATE ION, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | c-lectin crd, immune system, capsular polysaccharide. |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Total number of polymer chains | 4 |
| Total formula weight | 73810.66 |
| Authors | Silva-Martin, N.,Bartual, S.G.,Hermoso, J.A. (deposition date: 2012-12-21, release date: 2014-01-15, Last modification date: 2024-11-13) |
| Primary citation | Silva-Martin, N.,Bartual, S.G.,Ramirez-Aportela, E.,Chacon, P.,Park, C.G.,Hermoso, J.A. Structural Basis for Selective Recognition of Endogenous and Microbial Polysaccharides by Macrophage Receptor Sign-R1. Structure, 22:1595-, 2014 Cited by PubMed Abstract: SIGN-R1 is a principal receptor for microbial polysaccharides uptake and is responsible for C3 fixation via an unusual complement activation pathway on splenic marginal zone macrophages. In these macrophages, SIGN-R1 is also involved in anti-inflammatory activity of intravenous immunoglobulin by direct interaction with sialylated Fcs. The high-resolution crystal structures of SIGN-R1 carbohydrate recognition domain and its complexes with dextran sulfate or sialic acid, and of the sialylated Fc antibody provide insights into SIGN-R1’s selective recognition of a-2,6-sialylated glycoproteins. Unexpectedly, an additional binding site has been found in the SIGNR1 carbohydrate recognition domain, structurally separate from the calcium-dependent carbohydrate-binding site. This secondary binding site could bind repetitive molecular patterns, as observed in microbial polysaccharides, in a calcium-independent manner. These two binding sites may allow SIGNR1 to simultaneously bind both immune glycoproteins and microbial polysaccharide components, accommodating SIGN-R1’s ability to relate the recognition of microbes to the activation of the classical complement pathway. PubMed: 25450767DOI: 10.1016/J.STR.2014.09.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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