4CAJ
Crystallographic structure of the mouse SIGN-R1 CRD domain in complex with sialic acid
4CAJ の概要
エントリーDOI | 10.2210/pdb4caj/pdb |
関連するPDBエントリー | 4C9F |
分子名称 | CD209 ANTIGEN-LIKE PROTEIN B, CALCIUM ION, SULFATE ION, ... (6 entities in total) |
機能のキーワード | c-lectin crd, sign-r1, immune system, capsular polysaccharide |
由来する生物種 | MUS MUSCULUS (HOUSE MOUSE) |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 75934.12 |
構造登録者 | |
主引用文献 | Silva-Martin, N.,Bartual, S.G.,Rodriguez, A.,Ramirez, E.,Chacon, P.,Anthony, R.M.,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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.191 Å) |
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