Albumin
From Proteopedia
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<StructureSection load='' size='350' side='right' scene='Journal:JBSD:26/Cv/7' caption='Human serum albumin (PDB code [[1bm0]])'> | <StructureSection load='' size='350' side='right' scene='Journal:JBSD:26/Cv/7' caption='Human serum albumin (PDB code [[1bm0]])'> | ||
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| + | ==Function== | ||
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'''Albumin''' (Alb) is water-soluble protein. Serum albumin (SA) is the most abundant blood plasma protein. SA serves as carrier of fatty acids, bilirubin, ions and drugs. For details on human serum albumin see<br /> | '''Albumin''' (Alb) is water-soluble protein. Serum albumin (SA) is the most abundant blood plasma protein. SA serves as carrier of fatty acids, bilirubin, ions and drugs. For details on human serum albumin see<br /> | ||
*[[User:Neeharika Pothuri/Human Serum Albumin]]<br /> | *[[User:Neeharika Pothuri/Human Serum Albumin]]<br /> | ||
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*[[STRUCTURE 1BM0]]<br /> | *[[STRUCTURE 1BM0]]<br /> | ||
*[[Albumin (Hebrew)]]. | *[[Albumin (Hebrew)]]. | ||
| - | + | == Investigation on the Site-Selective Binding of Bovine Serum Albumin by Erlotinib Hydrochloride <ref>doi 10.1080/07391102.2012.726532</ref>== | |
The binding mode of <scene name='Journal:JBSD:26/Cv/2'>erlotinib hydrochloride (ET)</scene>, a targeted anticancer drug, to <scene name='Journal:JBSD:26/Cv/8'>bovine serum albumin (BSA)</scene> was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (<font color='red'><b>red for subdomain IA</b></font>; <span style="color:orange;background-color:black;font-weight:bold;">orange, IB</span>; <span style="color:cyan;background-color:black;font-weight:bold;">cyan, IIA</span>; <span style="color:yellow;background-color:black;font-weight:bold;">yellow, IIB</span>; <span style="color:lime;background-color:black;font-weight:bold;">green, IIIA</span>; <font color='darkmagenta'><b>darkmagenta, IIIB</b></font>). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the <scene name='Journal:JBSD:26/Cv/6'>binding site was located in the hydrophobic pocket of site I (subdomain IIA)</scene>. The docking modeling agreed with the results of the fluorescence and displacement experiments. | The binding mode of <scene name='Journal:JBSD:26/Cv/2'>erlotinib hydrochloride (ET)</scene>, a targeted anticancer drug, to <scene name='Journal:JBSD:26/Cv/8'>bovine serum albumin (BSA)</scene> was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (<font color='red'><b>red for subdomain IA</b></font>; <span style="color:orange;background-color:black;font-weight:bold;">orange, IB</span>; <span style="color:cyan;background-color:black;font-weight:bold;">cyan, IIA</span>; <span style="color:yellow;background-color:black;font-weight:bold;">yellow, IIB</span>; <span style="color:lime;background-color:black;font-weight:bold;">green, IIIA</span>; <font color='darkmagenta'><b>darkmagenta, IIIB</b></font>). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the <scene name='Journal:JBSD:26/Cv/6'>binding site was located in the hydrophobic pocket of site I (subdomain IIA)</scene>. The docking modeling agreed with the results of the fluorescence and displacement experiments. | ||
Revision as of 11:30, 3 March 2019
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3D Structures of albumin
Updated on 03-March-2019
References
- ↑ Liu Y, Chen M, Luo Z, Lin J, Song L. Investigation on the site-selective binding of bovine serum albumin by erlotinib hydrochloride. J Biomol Struct Dyn. 2012 Oct 17. PMID:23072300 doi:10.1080/07391102.2012.726532
