2bxc: Difference between revisions

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-[[Image:2bxc.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2bxc", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_2bxc|  PDB=2bxc  |  SCENE=  }}
-'''HUMAN SERUM ALBUMIN COMPLEXED WITH PHENYLBUTAZONE'''
+==Human serum albumin complexed with phenylbutazone==
+<StructureSection load='2bxc' size='340' side='right'caption='[[2bxc]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bxc]] is a 2 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=2BXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BXC FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P1Z:4-BUTYL-1,2-DIPHENYL-PYRAZOLIDINE-3,5-DIONE'>P1Z</scene></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=2bxc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxc OCA], [https://pdbe.org/2bxc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bxc RCSB], [https://www.ebi.ac.uk/pdbsum/2bxc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxc ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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 ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bx/2bxc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bxc ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Human serum albumin (HSA) is an abundant plasma protein that binds a remarkably wide range of drugs, thereby restricting their free, active concentrations. The problem of overcoming the binding affinity of lead compounds for HSA represents a major challenge in drug development. Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation. Numerous secondary binding sites for drugs distributed across the protein have also been identified. The binding of fatty acids, the primary physiological ligand for the protein, is shown to alter the polarity and increase the volume of drug site 1. These results clarify the interpretation of accumulated drug binding data and provide a valuable template for design efforts to modulate the interaction with HSA.
-==Overview==
+Structural basis of the drug-binding specificity of human serum albumin.,Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:16169013<ref>PMID:16169013</ref>
-Human serum albumin (HSA) is an abundant plasma protein that binds a remarkably wide range of drugs, thereby restricting their free, active concentrations. The problem of overcoming the binding affinity of lead compounds for HSA represents a major challenge in drug development. Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation. Numerous secondary binding sites for drugs distributed across the protein have also been identified. The binding of fatty acids, the primary physiological ligand for the protein, is shown to alter the polarity and increase the volume of drug site 1. These results clarify the interpretation of accumulated drug binding data and provide a valuable template for design efforts to modulate the interaction with HSA.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-BXC is a [[Single protein]] structure of 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=2BXC OCA].
+</div>
+<div class="pdbe-citations 2bxc" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis of the drug-binding specificity of human serum albumin., Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S, J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16169013 16169013]
+*[[Albumin 3D structures|Albumin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Bhattacharya, A A.]]
+[[Category: Bhattacharya AA]]
-[[Category: Curry, S.]]
+[[Category: Curry S]]
-[[Category: Ghuman, J.]]
+[[Category: Ghuman J]]
-[[Category: Petitpas, I.]]
+[[Category: Petitpas I]]
-[[Category: Zunszain, P A.]]
+[[Category: Zunszain PA]]
-[[Category: Metal-binding,drug-binding,phenylbutazone]]
-[[Category: Transport protein,albumin,carrier protein,lipid-binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:55:45 2008''