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2xsi, resolution 2.70Å ()
Ligands: ,
Related: 1hk4, 2bxq, 2bxi, 2xvu, 2vuf, 2xvv, 1o9x, 1bke, 2bxk, 1hk1, 1uor, 1h9z, 1e7b, 1hk2, 2esg, 1hk5, 1e7e, 2xvq, 2bxg, 2bxh, 2bxo, 2bxf, 1ysx, 1e7g, 2bxe, 2bxn, 1tf0, 2bxc, 1ao6, 1e7c, 1gnj, 2xw0, 1e7h, 2bxa, 1hk3, 2xvw, 1e7i, 2xw1, 2bxb, 1gni, 2bxl, 1ha2, 1bj5, 1e7a, 2bxp, 1bm0, 1e78, 2bxd, 2vdb, 1n5u, 1e7f, 2bxm, 2bx8, 2vue

Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Publication Abstract from PubMed

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.

Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin., Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S, J Struct Biol. 2010 Oct 18. PMID:20940056

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.


[ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.[1][2][3][4]


[ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.[5]

About this Structure

2xsi is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also


  • Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004
  1. Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S. An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. PMID:8048949
  2. Rushbrook JI, Becker E, Schussler GC, Divino CM. Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. PMID:7852505
  3. Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T. A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. PMID:9329347
  4. Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S. Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. PMID:9589637
  5. Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA. Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. doi: 10.1042/BST0361317. PMID:19021548 doi:10.1042/BST0361317

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