Journal:IUCrJ:S2052252522006820
From Proteopedia
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Serum albumin (SA) is the most abundant plasma protein and a transporter of hormones, metal ions, and common metabolites, such as fatty acids and sugars, in the blood<ref name='Doweiko'>doi: 10.1177/0148607191015002207</ref><ref name='Peters'>Peters TJT. All About Albumin: Biochemistry, Genetics, and Medical Applications. 1st ed. Academic Press; 1995 http://linkinghub.elsevier.com/retrieve/pii/B9780125521109X50004</ref>. Thanks to its highly flexible structure, and the presence of several binding sites that are able to accommodate a variety of small molecules, SA is also the major facilitator of vascular drug transport. Up to now, ten binding sites within albumin have been characterized as drug sites, and nine of these have been demonstrated to bind at least three FDA-approved drugs<ref name='Handing'>doi: 10.1021/acs.jmedchem.0c00225</ref>. Due to the high degree of structural conservation between mammalian albumins, non-human albumins, such as bovine serum albumin, or animal models, are often used to understand human albumin-drug interactions. | Serum albumin (SA) is the most abundant plasma protein and a transporter of hormones, metal ions, and common metabolites, such as fatty acids and sugars, in the blood<ref name='Doweiko'>doi: 10.1177/0148607191015002207</ref><ref name='Peters'>Peters TJT. All About Albumin: Biochemistry, Genetics, and Medical Applications. 1st ed. Academic Press; 1995 http://linkinghub.elsevier.com/retrieve/pii/B9780125521109X50004</ref>. Thanks to its highly flexible structure, and the presence of several binding sites that are able to accommodate a variety of small molecules, SA is also the major facilitator of vascular drug transport. Up to now, ten binding sites within albumin have been characterized as drug sites, and nine of these have been demonstrated to bind at least three FDA-approved drugs<ref name='Handing'>doi: 10.1021/acs.jmedchem.0c00225</ref>. Due to the high degree of structural conservation between mammalian albumins, non-human albumins, such as bovine serum albumin, or animal models, are often used to understand human albumin-drug interactions. | ||
| - | <scene name='94/949060/Cv/4'>The overall structure of HSA complex with ketoprofen</scene>. Albumin subdomains are each shown in a different color. Roman numerals (I, II, III) are associated with domains and letters (''e.g.,'' IB) with subdomains. Ketoprofen molecules are shown with atoms in white spheres. | + | <scene name='94/949060/Cv/4'>The overall structure of HSA complex with ketoprofen</scene>. <span class="bg-yellow"><span class="far fa-hand-point-right"></span> Remember to drag the structures with the mouse to rotate them.</span> Albumin subdomains are each shown in a different color. Roman numerals (I, II, III) are associated with domains and letters (''e.g.,'' IB) with subdomains. Ketoprofen molecules are shown with atoms in white spheres. |
Ketoprofen binding sites in HSA (PDB ID: [[7jwn]]): | Ketoprofen binding sites in HSA (PDB ID: [[7jwn]]): | ||
Revision as of 13:15, 31 January 2023
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
