1e7c: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e7c]] 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=1E7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E7C FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e7c]] 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=1E7C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E7C FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLT:2-BROMO-2-CHLORO-1,1,1-TRIFLUOROETHANE'>HLT</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HLT:2-BROMO-2-CHLORO-1,1,1-TRIFLUOROETHANE'>HLT</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ao6|1ao6]], [[1bj5|1bj5]], [[1bke|1bke]], [[1bm0|1bm0]], [[1e78|1e78]], [[1e7a|1e7a]], [[1e7b|1e7b]], [[1e7e|1e7e]], [[1e7f|1e7f]], [[1e7g|1e7g]], [[1e7h|1e7h]], [[1e7i|1e7i]], [[1uor|1uor]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ao6|1ao6]], [[1bj5|1bj5]], [[1bke|1bke]], [[1bm0|1bm0]], [[1e78|1e78]], [[1e7a|1e7a]], [[1e7b|1e7b]], [[1e7e|1e7e]], [[1e7f|1e7f]], [[1e7g|1e7g]], [[1e7h|1e7h]], [[1e7i|1e7i]], [[1uor|1uor]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e7c RCSB], [http://www.ebi.ac.uk/pdbsum/1e7c 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=1e7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1e7c RCSB], [http://www.ebi.ac.uk/pdbsum/1e7c PDBsum]</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> | [[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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bhattacharya, A A | [[Category: Bhattacharya, A A]] | ||
[[Category: Curry, S | [[Category: Curry, S]] | ||
[[Category: Franks, N P | [[Category: Franks, N P]] | ||
[[Category: General anesthetic]] | [[Category: General anesthetic]] | ||
[[Category: Halothane]] | [[Category: Halothane]] | ||
Revision as of 01:07, 23 December 2014
HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE GENERAL ANESTHETIC HALOTHANEHUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE GENERAL ANESTHETIC HALOTHANE
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 one of the most abundant proteins in the circulatory system and plays a key role in the transport of fatty acids, metabolites, and drugs. For many drugs, binding to serum albumin is a critical determinant of their distribution and pharmacokinetics; however, there have as yet been no high resolution crystal structures published of drug-albumin complexes. Here we describe high resolution crystal structures of HSA with two of the most widely used general anesthetics, propofol and halothane. In addition, we describe a crystal structure of HSA complexed with both halothane and the fatty acid, myristate. We show that the intravenous anesthetic propofol binds at two discrete sites on HSA in preformed pockets that have been shown to accommodate fatty acids. Similarly we show that the inhalational agent halothane binds (at concentrations in the pharmacologically relevant range) at three sites that are also fatty acid binding loci. At much higher halothane concentrations, we have identified additional sites that are occupied. All of the higher affinity anesthetic binding sites are amphiphilic in nature, with both polar and apolar parts, and anesthetic binding causes only minor changes in local structure. Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures.,Bhattacharya AA, Curry S, Franks NP J Biol Chem. 2000 Dec 8;275(49):38731-8. PMID:10940303[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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