6MDQ
Crystal structure of equine serum albumin in complex with testosterone
Summary for 6MDQ
| Entry DOI | 10.2210/pdb6mdq/pdb |
| Descriptor | Serum albumin, CITRATE ANION, TESTOSTERONE, ... (4 entities in total) |
| Functional Keywords | albumin, equine serum albumin, testosterone, csgid, structural genomics, center for structural genomics of infectious diseases, transport protein |
| Biological source | Equus caballus (Horse) |
| Total number of polymer chains | 1 |
| Total formula weight | 66912.23 |
| Authors | Czub, M.P.,Majorek, K.A.,Shabalin, I.G.,Handing, K.B.,Venkataramany, B.S.,Cymborowski, M.T.,Satchell, K.J.,Joachimiak, A.,Minor, W.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2018-09-05, release date: 2018-09-26, Last modification date: 2024-11-20) |
| Primary citation | Czub, M.P.,Venkataramany, B.S.,Majorek, K.A.,Handing, K.B.,Porebski, P.J.,Beeram, S.R.,Suh, K.,Woolfork, A.G.,Hage, D.S.,Shabalin, I.G.,Minor, W. Testosterone meets albumin - the molecular mechanism of sex hormone transport by serum albumins. Chem Sci, 10:1607-1618, 2019 Cited by PubMed Abstract: Serum albumin is the most abundant protein in mammalian blood plasma and is responsible for the transport of metals, drugs, and various metabolites, including hormones. We report the first albumin structure in complex with testosterone, the primary male sex hormone. Testosterone is bound in two sites, neither of which overlaps with the previously suggested Sudlow site I. We determined the binding constant of testosterone to equine and human albumins by two different methods: tryptophan fluorescence quenching and ultrafast affinity extraction. The binding studies and similarities between residues comprising the binding sites on serum albumins suggest that testosterone binds to the same sites on both proteins. Our comparative analysis of albumin complexes with hormones, drugs, and other biologically relevant compounds strongly suggests interference between a number of compounds present in blood and testosterone transport by serum albumin. We discuss a possible link between our findings and some phenomena observed in human patients, such as low testosterone levels in diabetic patients. PubMed: 30842823DOI: 10.1039/c8sc04397c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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