2MOG

Solution structure of the terminal Ig-like domain from Leptospira interrogans LigB

2MOG の概要

• エントリーDOI: 10.2210/pdb2mog/pdb
• NMR情報: BMRB: 19942
• 分子名称: Bacterial Ig-like domain, group 2 (1 entity in total)
• 機能のキーワード: immunoglobulin-like fold, surface protein, cell adhesion
• 由来する生物種: Leptospira interrogans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9641.49

構造登録者

Ptak, C.P.,Hsieh, C.,Lin, Y.,Maltsev, A.S.,Raman, R.,Sharma, Y.,Oswald, R.E.,Chang, Y. (登録日: 2014-04-25, 公開日: 2014-08-13, 最終更新日: 2024-05-15)

主引用文献

Ptak, C.P.,Hsieh, C.L.,Lin, Y.P.,Maltsev, A.S.,Raman, R.,Sharma, Y.,Oswald, R.E.,Chang, Y.F.
NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB.
Biochemistry, 53:5249-5260, 2014

PubMed Abstract: A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown promise as a marker in typing leptospiral isolates for pathogenesis and as an antigen in vaccines. We used NMR spectroscopy to solve the solution structure of the twelfth immunoglobulin-like (Ig-like) repeat domain from LigB (LigB-12). The fold is similar to that of other bacterial Ig-like domains and comprised mainly of β-strands that form a β-sandwich based on a Greek-key folding arrangement. Based on sequence analysis and conservation of structurally important residues, homology models for the other LigB Ig-like domains were generated. The set of LigB models illustrates the electrostatic differences between the domains as well as the possible interactions between neighboring domains. Understanding the structure of the extracellular portion of LigB and related proteins is important for developing diagnostic methods and new therapeutics directed toward leptospirosis.

PubMed: 25068811
DOI: 10.1021/bi500669u

実験手法

SOLUTION NMR