2fj9
From Proteopedia
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{{STRUCTURE_2fj9| PDB=2fj9 | SCENE= }} | {{STRUCTURE_2fj9| PDB=2fj9 | SCENE= }} | ||
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===High resolution crystal structure of the unliganded human ACBP=== | ===High resolution crystal structure of the unliganded human ACBP=== | ||
+ | {{ABSTRACT_PUBMED_17044054}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/ACBP_HUMAN ACBP_HUMAN]] 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. | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:017044054</ref><references group="xtra"/> | + | <ref group="xtra">PMID:017044054</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Aalten, D M.van.]] | [[Category: Aalten, D M.van.]] |
Revision as of 08:45, 23 April 2014
Contents |
High resolution crystal structure of the unliganded human ACBP
Template:ABSTRACT PUBMED 17044054
Function
[ACBP_HUMAN] 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.
About this Structure
2fj9 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Taskinen JP, van Aalten DM, Knudsen J, Wierenga RK. High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand. Proteins. 2007 Jan 1;66(1):229-38. PMID:17044054 doi:10.1002/prot.21124