4s1y
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==X-ray structure of human serum albumin complexed with cisplatin== |
+ | <StructureSection load='4s1y' size='340' side='right' caption='[[4s1y]], [[Resolution|resolution]] 3.16Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4s1y]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S1Y FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hk1|1hk1]]</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=4s1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4s1y RCSB], [http://www.ebi.ac.uk/pdbsum/4s1y PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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> | ||
+ | == 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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The reaction between cisplatin and human serum albumin (HSA) was investigated by X-ray crystallography and crystal structures of the cisplatin/HSA adduct were eventually solved for the first time. Structural data unambiguously prove that cisplatin mainly binds to His105 and Met329 side chains; additional binding sites are detected at His288, Met298, and Met548 and at His535, His67 and His247. | ||
- | + | Cisplatin binding to human serum albumin: a structural study.,Ferraro G, Massai L, Messori L, Merlino A Chem Commun (Camb). 2015 Apr 15. PMID:25873085<ref>PMID:25873085</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Merlino, A]] | [[Category: Merlino, A]] | ||
+ | [[Category: Albumin]] | ||
+ | [[Category: Drug transport]] | ||
+ | [[Category: Fatty acid]] | ||
+ | [[Category: Transport protein]] |
Revision as of 11:34, 30 April 2015
X-ray structure of human serum albumin complexed with cisplatin
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