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| - | ==HUMAN SERUM ALBUMIN COMPLEXED WITH DANSYL-L-GLUTAMATE AND MYRISTIC ACID== | + | |
| - | <StructureSection load='2xsi' size='340' side='right' caption='[[2xsi]], [[Resolution|resolution]] 2.70Å' scene=''> | + | ==Human serum albumin complexed with dansyl-L-glutamate and myristic acid== |
| | + | <StructureSection load='2xsi' size='340' side='right'caption='[[2xsi]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xsi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xsi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XSI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9NE:DANSYL-L-GLUTAMATE'>9NE</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hk4|1hk4]], [[2bxq|2bxq]], [[2bxi|2bxi]], [[2xvu|2xvu]], [[2vuf|2vuf]], [[2xvv|2xvv]], [[1o9x|1o9x]], [[1bke|1bke]], [[2bxk|2bxk]], [[1hk1|1hk1]], [[1uor|1uor]], [[1h9z|1h9z]], [[1e7b|1e7b]], [[1hk2|1hk2]], [[2esg|2esg]], [[1hk5|1hk5]], [[1e7e|1e7e]], [[2xvq|2xvq]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxo|2bxo]], [[2bxf|2bxf]], [[1ysx|1ysx]], [[1e7g|1e7g]], [[2bxe|2bxe]], [[2bxn|2bxn]], [[1tf0|1tf0]], [[2bxc|2bxc]], [[1ao6|1ao6]], [[1e7c|1e7c]], [[1gnj|1gnj]], [[2xw0|2xw0]], [[1e7h|1e7h]], [[2bxa|2bxa]], [[1hk3|1hk3]], [[2xvw|2xvw]], [[1e7i|1e7i]], [[2xw1|2xw1]], [[2bxb|2bxb]], [[1gni|1gni]], [[2bxl|2bxl]], [[1ha2|1ha2]], [[1bj5|1bj5]], [[1e7a|1e7a]], [[2bxp|2bxp]], [[1bm0|1bm0]], [[1e78|1e78]], [[2bxd|2bxd]], [[2vdb|2vdb]], [[1n5u|1n5u]], [[1e7f|1e7f]], [[2bxm|2bxm]], [[2bx8|2bx8]], [[2vue|2vue]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9NE:DANSYL-L-GLUTAMATE'>9NE</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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=2xsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xsi RCSB], [http://www.ebi.ac.uk/pdbsum/2xsi PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsi OCA], [https://pdbe.org/2xsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsi RCSB], [https://www.ebi.ac.uk/pdbsum/2xsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[http://omim.org/entry/103600 103600]]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref> | + | [https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[https://omim.org/entry/103600 103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.<ref>PMID:8048949</ref> <ref>PMID:7852505</ref> <ref>PMID:9329347</ref> <ref>PMID:9589637</ref> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref> | + | [https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2xsi" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Albumin|Albumin]] | + | *[[Albumin 3D structures|Albumin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Curry, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Ghuman, J]] | + | [[Category: Curry S]] |
| - | [[Category: Transport protein]] | + | [[Category: Ghuman J]] |
| Structural highlights
Disease
ALBU_HUMAN Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.[1] [2] [3] [4]
Function
ALBU_HUMAN Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.[5]
Publication Abstract from PubMed
Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.
Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin.,Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S J Struct Biol. 2010 Oct 18. PMID:20940056[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S. An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. PMID:8048949
- ↑ Rushbrook JI, Becker E, Schussler GC, Divino CM. Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. PMID:7852505
- ↑ Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T. A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. PMID:9329347
- ↑ Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S. Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. PMID:9589637
- ↑ Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA. Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. doi: 10.1042/BST0361317. PMID:19021548 doi:10.1042/BST0361317
- ↑ Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004
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