2XV9

The solution structure of ABA-1A saturated with oleic acid

2XV9 の概要

• エントリーDOI: 10.2210/pdb2xv9/pdb
• NMR情報: BMRB: 6333
• 分子名称: ABA-1A1 REPEAT UNIT (1 entity in total)
• 機能のキーワード: lipid binding protein, fatty acid binding, retinol binding, allergen
• 由来する生物種: ASCARIS SUUM (PIG ROUNDWORM)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15192.24

構造登録者

Smith, B.O.,Kennedy, M.W.,Cooper, A.,Meenan, N.A.G.,Bromek, K. (登録日: 2010-10-25, 公開日: 2011-08-10, 最終更新日: 2024-11-13)

主引用文献

Meenan, N.A.,Ball, G.,Bromek, K.,Uhrin, D.,Cooper, A.,Kennedy, M.W.,Smith, B.O.
Solution structure of a repeated unit of the ABA-1 nematode polyprotein allergen of Ascaris reveals a novel fold and two discrete lipid-binding sites.
PLoS Negl Trop Dis, 5:e1040-e1040, 2011

PubMed Abstract: Nematode polyprotein allergens (NPAs) are an unusual class of lipid-binding proteins found only in nematodes. They are synthesized as large, tandemly repetitive polyproteins that are post-translationally cleaved into multiple copies of small lipid binding proteins with virtually identical fatty acid and retinol (Vitamin A)-binding characteristics. They are probably central to transport and distribution of small hydrophobic compounds between the tissues of nematodes, and may play key roles in nutrient scavenging, immunomodulation, and IgE antibody-based responses in infection. In some species the repeating units are diverse in amino acid sequence, but, in ascarid and filarial nematodes, many of the units are identical or near-identical. ABA-1A is the most common repeating unit of the NPA of Ascaris suum, and is closely similar to that of Ascaris lumbricoides, the large intestinal roundworm of humans. Immune responses to NPAs have been associated with naturally-acquired resistance to infection in humans, and the immune repertoire to them is under strict genetic control.

PubMed: 21526216
DOI: 10.1371/journal.pntd.0001040

実験手法

SOLUTION NMR