6mdq: Difference between revisions
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==Crystal structure of equine serum albumin in complex with testosterone== | ==Crystal structure of equine serum albumin in complex with testosterone== | ||
<StructureSection load='6mdq' size='340' side='right' caption='[[6mdq]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='6mdq' size='340' side='right'caption='[[6mdq]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MDQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6mdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MDQ FirstGlance]. <br> | ||
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mdq OCA], [http://pdbe.org/6mdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mdq RCSB], [http://www.ebi.ac.uk/pdbsum/6mdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mdq ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6mdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mdq OCA], [http://pdbe.org/6mdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mdq RCSB], [http://www.ebi.ac.uk/pdbsum/6mdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mdq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Testosterone meets albumin - the molecular mechanism of sex hormone transport by serum albumins.,Czub MP, Venkataramany BS, Majorek KA, Handing KB, Porebski PJ, Beeram SR, Suh K, Woolfork AG, Hage DS, Shabalin IG, Minor W Chem Sci. 2018 Dec 17;10(6):1607-1618. doi: 10.1039/c8sc04397c. eCollection 2019 , Feb 14. PMID:30842823<ref>PMID:30842823</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6mdq" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Albumin 3D structures|Albumin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Large Structures]] | |||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Cymborowski, M T]] | [[Category: Cymborowski, M T]] | ||
Revision as of 11:19, 3 April 2019
Crystal structure of equine serum albumin in complex with testosteroneCrystal structure of equine serum albumin in complex with testosterone
Structural highlights
Publication Abstract from PubMedSerum 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. Testosterone meets albumin - the molecular mechanism of sex hormone transport by serum albumins.,Czub MP, Venkataramany BS, Majorek KA, Handing KB, Porebski PJ, Beeram SR, Suh K, Woolfork AG, Hage DS, Shabalin IG, Minor W Chem Sci. 2018 Dec 17;10(6):1607-1618. doi: 10.1039/c8sc04397c. eCollection 2019 , Feb 14. PMID:30842823[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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