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4WMO

Selenomethionine derivative of Xenopus laevis embryonic epidermal lectin carbohydrate-binding domain

4WMO の概要
エントリーDOI10.2210/pdb4wmo/pdb
関連するPDBエントリー4WN0
分子名称XEEL protein, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (4 entities in total)
機能のキーワードlectin, carbohydrate-binding protein, calcium, trimer, fibrinogen-like domain, x-type lectin, innate immunity, sugar binding protein
由来する生物種Xenopus laevis (African clawed frog)
細胞内の位置Secreted : Q5PPM0
タンパク質・核酸の鎖数6
化学式量合計195945.04
構造登録者
Wangkanont, K.,Kiessling, L.L.,Forest, K.T. (登録日: 2014-10-09, 公開日: 2016-01-20, 最終更新日: 2024-11-06)
主引用文献Wangkanont, K.,Wesener, D.A.,Vidani, J.A.,Kiessling, L.L.,Forest, K.T.
Structures of Xenopus Embryonic Epidermal Lectin Reveal a Conserved Mechanism of Microbial Glycan Recognition.
J.Biol.Chem., 291:5596-5610, 2016
Cited by
PubMed Abstract: Intelectins (X-type lectins), broadly distributed throughout chordates, have been implicated in innate immunity. Xenopus laevis embryonic epidermal lectin (XEEL), an intelectin secreted into environmental water by the X. laevis embryo, is postulated to function as a defense against microbes. XEEL is homologous (64% identical) to human intelectin-1 (hIntL-1), which is also implicated in innate immune defense. We showed previously that hIntL-1 binds microbial glycans bearing exocyclic vicinal diol groups. It is unknown whether XEEL has the same ligand specificity. Also unclear is whether XEEL and hIntL-1 have similar quaternary structures, as XEEL lacks the corresponding cysteine residues in hIntL-1 that stabilize the disulfide-linked trimer. These observations prompted us to further characterize XEEL. We found that hIntL-1 and XEEL have similar structural features. Even without the corresponding intermolecular disulfide bonds present in hIntL-1, the carbohydrate recognition domain of XEEL (XEELCRD) forms a stable trimer in solution. The structure of XEELCRD in complex with d-glycerol-1-phosphate, a residue present in microbe-specific glycans, indicated that the exocyclic vicinal diol coordinates to a protein-bound calcium ion. This ligand-binding mode is conserved between XEEL and hIntL-1. The domain architecture of full-length XEEL is reminiscent of a barbell, with two sets of three glycan-binding sites oriented in opposite directions. This orientation is consistent with our observation that XEEL can promote the agglutination of specific serotypes of Streptococcus pneumoniae. These data support a role for XEEL in innate immunity, and they highlight structural and functional conservation of X-type lectins among chordates.
PubMed: 26755729
DOI: 10.1074/jbc.M115.709212
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 4wmo
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-02-05に公開中

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