3G3B

Structure of a lamprey variable lymphocyte receptor mutant in complex with a protein antigen

3G3B の概要

• エントリーDOI: 10.2210/pdb3g3b/pdb
• 関連するPDBエントリー: 3G39 3G3A
• 分子名称: variable lymphocyte receptor VLRB.2D, Lysozyme C (3 entities in total)
• 機能のキーワード: vlr, antibody, allergen, antimicrobial, bacteriolytic enzyme, glycosidase, hydrolase, hydrolase-immune system complex, hydrolase/immune system
• 由来する生物種: Petromyzon marinus (Sea Lamprey); 詳細
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 132205.60

構造登録者

Deng, L.,Velikovsky, C.A.,Mariuzza, R.A. (登録日: 2009-02-02, 公開日: 2009-06-23, 最終更新日: 2024-11-06)

主引用文献

Velikovsky, C.A.,Deng, L.,Tasumi, S.,Iyer, L.M.,Kerzic, M.C.,Aravind, L.,Pancer, Z.,Mariuzza, R.A.
Structure of a lamprey variable lymphocyte receptor in complex with a protein antigen.
Nat.Struct.Mol.Biol., 16:725-730, 2009

PubMed Abstract: Variable lymphocyte receptors (VLRs) are leucine-rich repeat proteins that mediate adaptive immunity in jawless vertebrates. VLRs are fundamentally different from the antibodies of jawed vertebrates, which consist of immunoglobulin (Ig) domains. We determined the structure of an anti-hen egg white lysozyme (HEL) VLR, isolated by yeast display, bound to HEL. The VLR, whose affinity resembles that of IgM antibodies, uses nearly all its concave surface to bind the protein, in addition to a loop that penetrates into the enzyme active site. The VLR-HEL structure combined with sequence analysis revealed an almost perfect match between ligand-contacting positions and positions with highest sequence diversity. Thus, it is likely that we have defined the generalized antigen-binding site of VLRs. We further demonstrated that VLRs can be affinity-matured by 13-fold to affinities as high as those of IgG antibodies, making VLRs potential alternatives to antibodies for biotechnology applications.

PubMed: 19543291
DOI: 10.1038/nsmb.1619

実験手法

X-RAY DIFFRACTION (2.4 Å)