1JTB
LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES
Summary for 1JTB
Entry DOI | 10.2210/pdb1jtb/pdb |
Descriptor | LIPID TRANSFER PROTEIN, COENZYME A, PALMITIC ACID (3 entities in total) |
Functional Keywords | lipid transport, lipid transfer protein |
Biological source | Hordeum vulgare |
Total number of polymer chains | 1 |
Total formula weight | 10728.92 |
Authors | Lerche, M.H.,Kragelund, B.B.,Bech, L.M.,Poulsen, F.M. (deposition date: 1996-12-03, release date: 1997-07-07, Last modification date: 2024-10-16) |
Primary citation | Lerche, M.H.,Kragelund, B.B.,Bech, L.M.,Poulsen, F.M. Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands. Structure, 5:291-306, 1997 Cited by PubMed Abstract: . Plant nonspecific lipid-transfer proteins (nsLTPs) bind a variety of very different lipids in vitro, including phospholipids, glycolipids, fatty acids and acyl coenzyme As. In this study we have determined the structure of a nsLTP complexed with palmitoyl coenzyme A (PCoA) in order to further our understanding of the structural mechanism of the broad specificity of these proteins and its relation to the function of nsLTPs in vivo. PubMed: 9032083DOI: 10.1016/S0969-2126(97)00186-X PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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