2XV9
The solution structure of ABA-1A saturated with oleic acid
Summary for 2XV9
| Entry DOI | 10.2210/pdb2xv9/pdb |
| NMR Information | BMRB: 6333 |
| Descriptor | ABA-1A1 REPEAT UNIT (1 entity in total) |
| Functional Keywords | lipid binding protein, fatty acid binding, retinol binding, allergen |
| Biological source | ASCARIS SUUM (PIG ROUNDWORM) |
| Total number of polymer chains | 1 |
| Total formula weight | 15192.24 |
| Authors | Smith, B.O.,Kennedy, M.W.,Cooper, A.,Meenan, N.A.G.,Bromek, K. (deposition date: 2010-10-25, release date: 2011-08-10, Last modification date: 2024-11-13) |
| Primary citation | 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 Cited by 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: 21526216DOI: 10.1371/journal.pntd.0001040 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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