1b56
From Proteopedia
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| - | [[Image:1b56.gif|left|200px]] | + | [[Image:1b56.gif|left|200px]] |
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| - | '''HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN''' | + | {{Structure |
| + | |PDB= 1b56 |SIZE=350|CAPTION= <scene name='initialview01'>1b56</scene>, resolution 2.05Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PLM:PALMITIC ACID'>PLM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1B56 is a [ | + | 1B56 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B56 OCA]. |
==Reference== | ==Reference== | ||
| - | Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein., Hohoff C, Borchers T, Rustow B, Spener F, van Tilbeurgh H, Biochemistry. 1999 Sep 21;38(38):12229-39. PMID:[http:// | + | Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein., Hohoff C, Borchers T, Rustow B, Spener F, van Tilbeurgh H, Biochemistry. 1999 Sep 21;38(38):12229-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10493790 10493790] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipid-binding]] | [[Category: lipid-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:06:28 2008'' |
Revision as of 08:06, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN RECOMBINANT EPIDERMAL FATTY ACID BINDING PROTEIN
Overview
We describe the crystal structure of human epidermal-type fatty acid binding protein (E-FABP) that was recently found to be highly upregulated in human psoriatic keratinocytes. To characterize E-FABP with respect to ligand-binding properties and tertiary structure, we cloned the respective cDNA, overexpressed the protein in Escherichia coli and purified it to homogeneity by a combination of ion-exchange and size-exclusion chromatographic steps with a yield of 30 mg/L broth. The purified protein revealed a 5-fold higher affinity for stearic acid than for oleic and arachidonic acids. The crystal structure of recombinant human E-FABP was determined to 2.05 A and refined to an R(factor) of 20.7%. The initial residual electron density maps clearly showed the presence of a ligand, which was identified as endogenous bacterial fatty acid. Within a central cavity of 252 A(3), this ligand is bound in a U-shaped conformation, its carboxyl group interacting with tyrosine 131 and arginines 129 and 109, the latter via an ordered water molecule. The E-FABP crystal structure is unique in the FABP family because of the presence of a disulfide bridge between cysteines 120 and 127 that may be physiologically as well as pathophysiologically relevant. Cysteines 67 and 87 are also in close vicinity but in contrast do not form a disulfide bridge. We postulate that this protein belongs to a particular FABP subfamily whose members share common structural as well as functional features.
About this Structure
1B56 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein., Hohoff C, Borchers T, Rustow B, Spener F, van Tilbeurgh H, Biochemistry. 1999 Sep 21;38(38):12229-39. PMID:10493790
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