3LEK
Lectin Domain of Lectinolysin complexed with Lewis B Antigen
3LEK の概要
エントリーDOI | 10.2210/pdb3lek/pdb |
関連するPDBエントリー | 3LEG 3LEI 3LEO |
関連するBIRD辞書のPRD_ID | PRD_900085 |
分子名称 | Platelet aggregation factor Sm-hPAF, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-3)-[alpha-L-fucopyranose-(1-4)]2-acetamido-2-deoxy-alpha-D-glucopyranose, CALCIUM ION, ... (5 entities in total) |
機能のキーワード | lectin domain of lectinolysin, lewis b antigen, blood clotting, nickel |
由来する生物種 | Streptococcus mitis |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 17641.88 |
構造登録者 | |
主引用文献 | Feil, S.C.,Lawrence, S.,Mulhern, T.D.,Holien, J.K.,Hotze, E.M.,Farrand, S.,Tweten, R.K.,Parker, M.W. Structure of the lectin regulatory domain of the cholesterol-dependent cytolysin lectinolysin reveals the basis for its lewis antigen specificity. Structure, 20:248-258, 2012 Cited by PubMed Abstract: The cholesterol-dependent cytolysins (CDCs) punch holes in target cell membranes through a highly regulated process. Streptococcus mitis lectinolysin (LLY) exhibits another layer of regulation with a lectin domain that enhances the pore-forming activity of the toxin. We have determined the crystal structures of the lectin domain by itself and in complex with various glycans that reveal the molecular basis for the Lewis antigen specificity of LLY. A small-angle X-ray scattering study of intact LLY reveals the molecule is flat and elongated with the lectin domain oriented so that the Lewis antigen-binding site is exposed. We suggest that the lectin domain enhances the pore-forming activity of LLY by concentrating toxin molecules at fucose-rich sites on membranes, thus promoting the formation of prepore oligomers on the surface of susceptible cells. PubMed: 22325774DOI: 10.1016/j.str.2011.11.017 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード
