1bj5: Difference between revisions
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==HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID== | ==HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID== | ||
<StructureSection load='1bj5' size='340' side='right' caption='[[1bj5]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1bj5' size='340' side='right' caption='[[1bj5]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bj5]] is a 1 chain structure | <table><tr><td colspan='2'>[[1bj5]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BJ5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=1bj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bj5 OCA], [http://pdbe.org/1bj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bj5 RCSB], [http://www.ebi.ac.uk/pdbsum/1bj5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bj5 ProSAT]</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=1bj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bj5 OCA], [http://pdbe.org/1bj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bj5 RCSB], [http://www.ebi.ac.uk/pdbsum/1bj5 PDBsum]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1bj5 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brick, P]] | [[Category: Brick, P]] | ||
[[Category: Curry, S]] | [[Category: Curry, S]] | ||
Revision as of 09:14, 17 August 2017
HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACIDHUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID
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] 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 PubMedHuman serum albumin (HSA) is the most abundant protein in the circulatory system. Its principal function is to transport fatty acids, but it is also capable of binding a great variety of metabolites and drugs. Despite intensive efforts, the detailed structural basis of fatty acid binding to HSA has remained elusive. We have now determined the crystal structure of HSA complexed with five molecules of myristate at 2.5 A resolution. The fatty acid molecules bind in long, hydrophobic pockets capped by polar side chains, many of which are basic. These pockets are distributed asymmetrically throughout the HSA molecule, despite its symmetrical repeating domain structure. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites.,Curry S, Mandelkow H, Brick P, Franks N Nat Struct Biol. 1998 Sep;5(9):827-35. PMID:9731778[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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