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PDBsum entry 3p6c
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Lipid binding protein
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PDB id
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3p6c
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PDB id:
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| Name: |
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Lipid binding protein
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Title:
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Human adipocyte lipid-binding protein fabp4 in complex with citric acid
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Structure:
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Fatty acid-binding protein, adipocyte. Chain: a. Synonym: adipocyte lipid-binding protein, albp, adipocyte-type fatty acid-binding protein, a-fabp, afabp, fatty acid-binding protein 4. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: fabp4. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.25Å
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R-factor:
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0.171
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R-free:
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0.212
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Authors:
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J.M.Gonzalez,E.Pozharski
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Key ref:
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J.M.González
and
S.Z.Fisher
(2015).
Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).
Acta Crystallogr F Struct Biol Commun,
71,
163-170.
PubMed id:
DOI:
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Date:
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11-Oct-10
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Release date:
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13-Apr-11
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PROCHECK
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Headers
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References
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P15090
(FABP4_HUMAN) -
Fatty acid-binding protein, adipocyte from Homo sapiens
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Seq:
Struc:
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132 a.a.
139 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Acta Crystallogr F Struct Biol Commun
71:163-170
(2015)
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PubMed id:
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Structural analysis of ibuprofen binding to human adipocyte fatty-acid binding protein (FABP4).
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J.M.González,
S.Z.Fisher.
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ABSTRACT
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Inhibition of human adipocyte fatty-acid binding protein (FABP4) has been
proposed as a treatment for type 2 diabetes, fatty liver disease and
atherosclerosis. However, FABP4 displays a naturally low selectivity towards
hydrophobic ligands, leading to the possibility of side effects arising from
cross-inhibition of other FABP isoforms. In a search for structural determinants
of ligand-binding selectivity, the binding of FABP4 towards a group of small
molecules structurally related to the nonsteroidal anti-inflammatory drug
ibuprofen was analyzed through X-ray crystallography. Several specific
hydrophobic interactions are shown to enhance the binding affinities of these
compounds, whereas an aromatic edge-to-face interaction is proposed to determine
the conformation of bound ligands, highlighting the importance of aromatic
interactions in hydrophobic environments.
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Links
