| Home > Publications database > Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. |
| Journal Article | PHPPUBDB-19273 |
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2011
Elsevier
San Diego, Calif.
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Please use a persistent id in citations: doi:10.1016/j.jsb.2010.10.004
Abstract: Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.
Keyword(s): Arginine: analogs & derivatives (MeSH) ; Arginine: metabolism (MeSH) ; Asparagine: analogs & derivatives (MeSH) ; Asparagine: metabolism (MeSH) ; Dansyl Compounds: metabolism (MeSH) ; Glutamates: metabolism (MeSH) ; Humans (MeSH) ; Phenylalanine: metabolism (MeSH) ; Protein Binding (MeSH) ; Sarcosine: analogs & derivatives (MeSH) ; Sarcosine: metabolism (MeSH) ; Serum Albumin: metabolism (MeSH) ; Dansyl Compounds ; Glutamates ; Serum Albumin ; dansyl-phenylalanine ; Sarcosine ; dansylsarcosine ; dansyl asparagine ; dansyl-L-arginine ; Phenylalanine ; dansylglutamic acid ; Asparagine ; Arginine
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