2vuf

From Proteopedia

(Difference between revisions)

Revision as of 20:45, 19 September 2018

Human serum albumin complexed with fusidic acid

Structural highlights

2vuf is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bxq, 1hk4, 2bxi, 1o9x, 1bke, 2bxk, 1uor, 1hk1, 1h9z, 1e7b, 1hk2, 1hk5, 2esg, 1e7e, 2bxg, 2bxh, 2bxo, 2bxf, 1ysx, 1e7g, 2bxc, 1tf0, 1ao6, 2bxe, 2bxn, 1e7c, 1gnj, 1e7h, 2bxa, 1hk3, 2bxb, 1e7i, 2bxl, 1gni, 1ha2, 1bj5, 1e7a, 2bxp, 2bxd, 1e78, 1bm0, 2vdb, 1n5u, 1e7f, 2bx8, 2bxm, 2vue
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bilirubin, an insoluble yellow-orange pigment derived from heme catabolism, accumulates to toxic levels in individuals with impaired or immature liver function. The resulting jaundice may be managed with phototherapy to isomerize the biosynthetic 4Z,15Z-bilirubin-IXalpha to more soluble and excretable isomers, such as 4Z,15E-bilirubin. Bilirubin and its configurational isomers are transported to the liver by human serum albumin (HSA) but their precise binding location(s) on the protein have yet to be determined. To investigate the molecular details of their interaction, we co-crystallised bilirubin with HSA. Strikingly, the crystal structure--determined to 2.42 A resolution--revealed the 4Z,15E-bilirubin-IXalpha isomer bound to an L-shaped pocket in sub-domain IB. We also determined the co-crystal structure of HSA complexed with fusidic acid, an antibiotic that competitively displaces bilirubin from the protein, and showed that it binds to the same pocket. These results provide the first crystal structure of a natural bilirubin pigment bound to serum albumin, challenge some of the present conceptions about HSA-bilirubin interactions, and provide a sound structural framework for finally resolving the long-standing question of where 4Z,15Z-bilirubin-IXalpha binds to the protein.

Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXalpha.,Zunszain PA, Ghuman J, McDonagh AF, Curry S J Mol Biol. 2008 Aug 29;381(2):394-406. Epub 2008 Jun 12. PMID:18602119^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Zunszain PA, Ghuman J, McDonagh AF, Curry S. Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXalpha. J Mol Biol. 2008 Aug 29;381(2):394-406. Epub 2008 Jun 12. PMID:18602119 doi:http://dx.doi.org/10.1016/j.jmb.2008.06.016

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vuf"

@@ Line 1: / Line 1: @@
-==HUMAN SERUM ALBUMIN COMPLEXED WITH FUSIDIC ACID==
+==Human serum albumin complexed with fusidic acid==
 <StructureSection load='2vuf' size='340' side='right' caption='[[2vuf]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FUA:FUSIDIC+ACID'>FUA</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bxq|2bxq]], [[1hk4|1hk4]], [[2bxi|2bxi]], [[1o9x|1o9x]], [[1bke|1bke]], [[2bxk|2bxk]], [[1uor|1uor]], [[1hk1|1hk1]], [[1h9z|1h9z]], [[1e7b|1e7b]], [[1hk2|1hk2]], [[1hk5|1hk5]], [[2esg|2esg]], [[1e7e|1e7e]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxo|2bxo]], [[2bxf|2bxf]], [[1ysx|1ysx]], [[1e7g|1e7g]], [[2bxc|2bxc]], [[1tf0|1tf0]], [[1ao6|1ao6]], [[2bxe|2bxe]], [[2bxn|2bxn]], [[1e7c|1e7c]], [[1gnj|1gnj]], [[1e7h|1e7h]], [[2bxa|2bxa]], [[1hk3|1hk3]], [[2bxb|2bxb]], [[1e7i|1e7i]], [[2bxl|2bxl]], [[1gni|1gni]], [[1ha2|1ha2]], [[1bj5|1bj5]], [[1e7a|1e7a]], [[2bxp|2bxp]], [[2bxd|2bxd]], [[1e78|1e78]], [[1bm0|1bm0]], [[2vdb|2vdb]], [[1n5u|1n5u]], [[1e7f|1e7f]], [[2bx8|2bx8]], [[2bxm|2bxm]], [[2vue|2vue]]</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=2vuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vuf OCA], [http://pdbe.org/2vuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vuf RCSB], [http://www.ebi.ac.uk/pdbsum/2vuf PDBsum]</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=2vuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vuf OCA], [http://pdbe.org/2vuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vuf RCSB], [http://www.ebi.ac.uk/pdbsum/2vuf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vuf ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vu/2vuf_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vu/2vuf_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 42: / Line 43: @@
 [[Category: Zunszain, P A]]
 [[Category: Albumin]]
+[[Category: Alternative splicing]]
 [[Category: Carrier protein]]
 [[Category: Cleavage on pair of basic residue]]
+[[Category: Copper]]
 [[Category: Disease mutation]]
 [[Category: Drug-binding]]
@@ Line 51: / Line 54: @@
 [[Category: Lipid-binding]]
 [[Category: Metal-binding]]
+[[Category: Polymorphism]]
 [[Category: Secreted]]
 [[Category: Transport protein]]

2vuf

From Proteopedia

Revision as of 20:45, 19 September 2018

Human serum albumin complexed with fusidic acid

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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