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1JTB

LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES

Summary for 1JTB
Entry DOI10.2210/pdb1jtb/pdb
DescriptorLIPID TRANSFER PROTEIN, COENZYME A, PALMITIC ACID (3 entities in total)
Functional Keywordslipid transport, lipid transfer protein
Biological sourceHordeum vulgare
Total number of polymer chains1
Total formula weight10728.92
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 citationLerche, 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: 9032083
DOI: 10.1016/S0969-2126(97)00186-X
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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