Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin

Ali J. Ryan, Jamie Ghuman, Patricia A. Zunszain, Chun wa Chung, Stephen Curry*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

108 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)84-91
Number of pages8
JournalJournal of Structural Biology
Volume174
Issue number1
DOIs
Publication statusPublished - 1 Apr 2011
Externally publishedYes

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