1aca

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THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME ATHREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A

Structural highlights

1aca is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACBP_BOVIN Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287 doi:10.1006/jmbi.2001.4749
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