3lu6

From Proteopedia

(Difference between revisions)

Revision as of 19:19, 5 August 2016

Human serum albumin in complex with compound 1

Structural highlights

3lu6 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3lu7, 3lu8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

The displacement of probes that bind selectively to subdomains IIA or IIIA on human serum albumin (HSA) by competing compounds has been followed using fluorescence spectroscopy, and has therefore been used to assign a primary binding site for these compounds in the presence and absence of fatty acids. The crystal structures have also been solved for three compounds: a matched pair of carboxylic acids whose binding strength to HSA unexpectedly decreased as the lipophilicity increased; and a highly bound sulphonamide that appeared not to displace the probes in the displacement assay. The crystallography results support the findings from the fluorescence displacement assay. The results indicate that drug binding to subdomain IB might also be important location for certain compounds.

A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions.,Buttar D, Colclough N, Gerhardt S, MacFaul PA, Phillips SD, Plowright A, Whittamore P, Tam K, Maskos K, Steinbacher S, Steuber H Bioorg Med Chem. 2010 Nov 1;18(21):7486-96. Epub 2010 Sep 24. PMID:20869876^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S. An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. PMID:8048949
↑ Rushbrook JI, Becker E, Schussler GC, Divino CM. Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. PMID:7852505
↑ Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T. A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. PMID:9329347
↑ Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S. Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. PMID:9589637
↑ Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA. Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. doi: 10.1042/BST0361317. PMID:19021548 doi:10.1042/BST0361317
↑ Buttar D, Colclough N, Gerhardt S, MacFaul PA, Phillips SD, Plowright A, Whittamore P, Tam K, Maskos K, Steinbacher S, Steuber H. A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions. Bioorg Med Chem. 2010 Nov 1;18(21):7486-96. Epub 2010 Sep 24. PMID:20869876 doi:10.1016/j.bmc.2010.08.052

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lu6"

@@ Line 1: / Line 1: @@
 ==Human serum albumin in complex with compound 1==
 <StructureSection load='3lu6' size='340' side='right' caption='[[3lu6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMX:[(1R,2R)-2-{[(5-FLUORO-1H-INDOL-2-YL)CARBONYL]AMINO}-2,3-DIHYDRO-1H-INDEN-1-YL]ACETIC+ACID'>IMX</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lu7|3lu7]], [[3lu8|3lu8]]</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=3lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lu6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lu6 RCSB], [http://www.ebi.ac.uk/pdbsum/3lu6 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=3lu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lu6 OCA], [http://pdbe.org/3lu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lu6 RCSB], [http://www.ebi.ac.uk/pdbsum/3lu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lu6 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3lu6" style="background-color:#fffaf0;"></div>
 ==See Also==

3lu6

From Proteopedia

Revision as of 19:19, 5 August 2016

Human serum albumin in complex with compound 1

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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