4l9q: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l9q]] 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=4L9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L9Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l9q]] 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=4L9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L9Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9TP:(5S,5AR,8AR,9R)-9-(4-HYDROXY-3,5-DIMETHOXYPHENYL)-8-OXO-5,5A,6,8,8A,9-HEXAHYDROFURO[3,4 6,7]NAPHTHO[2,3-D][1,3]DIOXOL-5-YL+4,6-O-(THIOPHEN-2-YLMETHYLIDENE)-BETA-D-GLUCOPYRANOSIDE'>9TP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9TP:(5S,5AR,8AR,9R)-9-(4-HYDROXY-3,5-DIMETHOXYPHENYL)-8-OXO-5,5A,6,8,8A,9-HEXAHYDROFURO[3,4 6,7]NAPHTHO[2,3-D][1,3]DIOXOL-5-YL+4,6-O-(THIOPHEN-2-YLMETHYLIDENE)-BETA-D-GLUCOPYRANOSIDE'>9TP</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=4l9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9q OCA], [https://pdbe.org/4l9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l9q RCSB], [https://www.ebi.ac.uk/pdbsum/4l9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9q ProSAT]</span></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=4l9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9q OCA], [https://pdbe.org/4l9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l9q RCSB], [https://www.ebi.ac.uk/pdbsum/4l9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l9q ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== 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>  
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Serum albumin is a major pharmacokinetic effector of drugs. To gain further insight into albumin binding chemistry, the crystal structures of six oncology agents were determined in complex with human serum albumin at resolutions of 2.8 to 2.0A: camptothecin, 9-amino-camptothecin, etoposide, teniposide, bicalutamide and idarubicin. METHODS: Protein crystal growth and low temperature X-ray crystallography RESULTS: These large, complex drugs are all bound within the subdomain IB binding region which can be described as a hydrophobic groove formed by alpha-helices h7, h8 and h9 covered by the extended polypeptide L1. L1 creates a binding cavity with two access sites, one between loop L1 and alpha-helices h7 and h8 (distal site: IBd) and the other between L1 and alpha-helix h9 (proximal site: IBp). Camptothecin (2.4A) and 9 amino camptothecin (2.0A) are clearly bound as the open lactone form (IBp). Idarubicin (2.8A) binds in a DNA like dimer complex via an intermolecular pi stacking arrangement in IBd. Bicalutamide (2.4A) is bound in a folded intramolecular pi stacking arrangement between two aromatic rings in IBd similar to idarubicin. Teniposide (2.7A) and etoposide (2.7A), despite small chemical differences, are bound in two distinctly different sites at or near IB. Teniposide is internalized via primarily hydrophobic interactions and spans through both openings (IBp-d). Etoposide is bound between the exterior of IB and IIA and exhibits an extensive hydrogen bonding network. CONCLUSIONS: Subdomain IB is a major binding site for complex heterocyclic molecules. GENERAL SIGNIFICANCE: The structures have important implications for drug design and development. This article is part of a Special Issue entitled Serum Albumin.
Structural studies of several clinically important oncology drugs in complex with human serum albumin.,Wang ZM, Ho JX, Ruble JR, Rose J, Ruker F, Ellenburg M, Murphy R, Click J, Soistman E, Wilkerson L, Carter DC Biochim Biophys Acta. 2013 Jul 6. pii: S0304-4165(13)00292-4. doi:, 10.1016/j.bbagen.2013.06.032. PMID:23838380<ref>PMID:23838380</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4l9q" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Retrieved from "https://proteopedia.org/4l9q"