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| **[[3b9m]] - hSA + AZT + salicylic acid + myristic acid<br /> | | **[[3b9m]] - hSA + AZT + salicylic acid + myristic acid<br /> |
| **[[2vdb]] - hSA + peptostreptococcal albumin-binding protein GA module + naproxen<br /> | | **[[2vdb]] - hSA + peptostreptococcal albumin-binding protein GA module + naproxen<br /> |
| **[[4k71]], [[4n0f]] – hSA + Igg receptpr + β-2-microglobulin<br /> | | **[[4k71]], [[4n0f]] – hSA + Igg receptor + β-2-microglobulin<br /> |
| **[[4n0u]] – hSA + Igg receptpr + β-2-microglobulin + Ig γ-1 chain C<br /> | | **[[4n0u]] – hSA + Igg receptor + β-2-microglobulin + Ig γ-1 chain C<br /> |
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| *Other serum albumins | | *Other serum albumins |
Revision as of 21:00, 17 December 2017
| 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
Investigation on the Site-Selective Binding of Bovine Serum Albumin by Erlotinib Hydrochloride [1]
The binding mode of erlotinib hydrochloride (ET), a targeted anticancer drug, to bovine serum albumin (BSA) was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (red for subdomain IA; orange, IB; cyan, IIA; yellow, IIB; green, IIIA; darkmagenta, IIIB). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the binding site was located in the hydrophobic pocket of site I (subdomain IIA). The docking modeling agreed with the results of the fluorescence and displacement experiments.
- ↑ 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
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3D Structures of albumin
Updated on 17-December-2017
{"openlevels":0}
- Human serum albumin
- Human serum albumin binary complex
- 2ydf – hSA + iophenoxic acid
- 2xvq, 2xvu, 2xw0, 2xw1 - hSA + dansyl derivative
- 3lu6, 3ju7, 3lu8, 2bx8, 2bxa, 2bxb, 2bxc, 2bxd, 2bxe, 2bxf, 2bxg, 2bxh, 2bxi, 2bxk, 2bxl, 2bxm, 2bxn,2bxo, 2bxp, 2bxq, 3lu7, 4l8u, 4l9k, 4l9q, 4la0, 4lb2, 4lb9, 5ifo, 5id9, 5id7 – hSA + drug
- 4iw1, 4iw2 – hSA + monosaccharide
- 3jqz – hSA + lidocaine
- 3jry - hSA + sulfate
- 4emx – hSA + Cl
- 5ifj, 5ije, 5ij5, 5iix, 5iiu, 5iih – hSA + Zn
- 4s1y – hSA + cisplatin
- 1n5u - hSA + heme
- 3a73 - hSA + prostaglandin
- 2vuf, 2vue - hSA + bilirubin derivative
- 1gni, 1gnj, 1e7h, 1e7e, 1e7f, 1e7i, 1bke, 1bj5, 3tdl, 4e99, 4bke - hSA + fatty acid
- 1hk1 - hSA + thiroxine
- 2hk2, 1hk3, 1hk2 - hSA (mutant) + thiroxine
- 1e7a, 1e7b - hSA + general anesthetic
- 1tf0 - hSA + peptostreptococcal albumin-binding protein GA module
- 2esg - hSA + immunoglobulin A1
- 1ysx - hSA + anti-apoptotic ligand – NMR
- 4hgk, 4hgm, 5fuo – hSA + shark antibody
- Human serum albumin ternary complex
- 2xsi, 2xvv, 2xvw – hSA + dansyl derivative + myristic acid
- 3cx9 - hSA + lysophospholipid + myristic acid
- 1e7g - hSA + fatty acid + myristic acid
- 1h9z, 1ha2 - hSA + warfarine + myristic acid
- 1e7c - hSA + general anesthetic + myristic acid
- 1hk4 - hSA + thiroxine + myristic acid
- 1hk5 - hSA (mutant) + thiroxine + myristic acid
- 1o9x - hSA + hemin + myristic acid
- 3uiv - hSA + amantadine + myristic acid
- 3b9l - hSA + AZT + myristic acid
- 2i2z - hSA + aspirin + myristic acid
- 2i30 - hSA + salicylic acid + myristic acid
- 4z69 – hSA + palmitate + diclofenac
- 3b9m - hSA + AZT + salicylic acid + myristic acid
- 2vdb - hSA + peptostreptococcal albumin-binding protein GA module + naproxen
- 4k71, 4n0f – hSA + Igg receptor + β-2-microglobulin
- 4n0u – hSA + Igg receptor + β-2-microglobulin + Ig γ-1 chain C
- Other serum albumins
- Albumin
- 1s6d – Alb 8 – sunflower – NMR
- 1wba – Alb 1 – winged bean
- 1p8b – Alb 1 – pea
- 1psy – Alb – castor bean - NMR
- 3lp9 – Alb hemopexin domain – Lathyrus sativus
- 2lvf – Alb – Brazil nut
- 5dom – SA 2S – horseradish tree
References
proteopedia link