2bxk

From Proteopedia

(Difference between revisions)

Revision as of 12:11, 27 April 2022

Human serum albumin complexed with myristate, azapropazone and indomethacin

Structural highlights

2bxk is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1ao6, 1bj5, 1bke, 1bm0, 1e78, 1e7a, 1e7b, 1e7c, 1e7e, 1e7f, 1e7g, 1e7h, 1e7i, 1gni, 1gnj, 1h9z, 1ha2, 1hk1, 1hk2, 1hk3, 1hk4, 1hk5, 1n5u, 1o9x, 1tf0, 1uor, 1ysx, 2bx8, 2bxa, 2bxb, 2bxc, 2bxd, 2bxe, 2bxf, 2bxg, 2bxh, 2bxi, 2bxl, 2bxm, 2bxn, 2bxo, 2bxp, 2bxq
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]

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 PubMed

Human serum albumin (HSA) is an abundant plasma protein that binds a remarkably wide range of drugs, thereby restricting their free, active concentrations. The problem of overcoming the binding affinity of lead compounds for HSA represents a major challenge in drug development. Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation. Numerous secondary binding sites for drugs distributed across the protein have also been identified. The binding of fatty acids, the primary physiological ligand for the protein, is shown to alter the polarity and increase the volume of drug site 1. These results clarify the interpretation of accumulated drug binding data and provide a valuable template for design efforts to modulate the interaction with HSA.

Structural basis of the drug-binding specificity of human serum albumin.,Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:16169013^[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
↑ Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S. Structural basis of the drug-binding specificity of human serum albumin. J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:16169013 doi:http://dx.doi.org/10.1016/j.jmb.2005.07.075

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bxk"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bxk' size='340' side='right'caption='[[2bxk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bxk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BXK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2BXK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bxk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BXK FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZQ:AZAPROPAZONE'>AZQ</scene>, <scene name='pdbligand=IMN:INDOMETHACIN'>IMN</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></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]], [[1e7c|1e7c]], [[1e7e|1e7e]], [[1e7f|1e7f]], [[1e7g|1e7g]], [[1e7h|1e7h]], [[1e7i|1e7i]], [[1gni|1gni]], [[1gnj|1gnj]], [[1h9z|1h9z]], [[1ha2|1ha2]], [[1hk1|1hk1]], [[1hk2|1hk2]], [[1hk3|1hk3]], [[1hk4|1hk4]], [[1hk5|1hk5]], [[1n5u|1n5u]], [[1o9x|1o9x]], [[1tf0|1tf0]], [[1uor|1uor]], [[1ysx|1ysx]], [[2bx8|2bx8]], [[2bxa|2bxa]], [[2bxb|2bxb]], [[2bxc|2bxc]], [[2bxd|2bxd]], [[2bxe|2bxe]], [[2bxf|2bxf]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxi|2bxi]], [[2bxl|2bxl]], [[2bxm|2bxm]], [[2bxn|2bxn]], [[2bxo|2bxo]], [[2bxp|2bxp]], [[2bxq|2bxq]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ao6|1ao6]], [[1bj5|1bj5]], [[1bke|1bke]], [[1bm0|1bm0]], [[1e78|1e78]], [[1e7a|1e7a]], [[1e7b|1e7b]], [[1e7c|1e7c]], [[1e7e|1e7e]], [[1e7f|1e7f]], [[1e7g|1e7g]], [[1e7h|1e7h]], [[1e7i|1e7i]], [[1gni|1gni]], [[1gnj|1gnj]], [[1h9z|1h9z]], [[1ha2|1ha2]], [[1hk1|1hk1]], [[1hk2|1hk2]], [[1hk3|1hk3]], [[1hk4|1hk4]], [[1hk5|1hk5]], [[1n5u|1n5u]], [[1o9x|1o9x]], [[1tf0|1tf0]], [[1uor|1uor]], [[1ysx|1ysx]], [[2bx8|2bx8]], [[2bxa|2bxa]], [[2bxb|2bxb]], [[2bxc|2bxc]], [[2bxd|2bxd]], [[2bxe|2bxe]], [[2bxf|2bxf]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxi|2bxi]], [[2bxl|2bxl]], [[2bxm|2bxm]], [[2bxn|2bxn]], [[2bxo|2bxo]], [[2bxp|2bxp]], [[2bxq|2bxq]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxk OCA], [http://pdbe.org/2bxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bxk RCSB], [http://www.ebi.ac.uk/pdbsum/2bxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxk 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=2bxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bxk OCA], [https://pdbe.org/2bxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bxk RCSB], [https://www.ebi.ac.uk/pdbsum/2bxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bxk ProSAT]</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>
+[[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN]] Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:[https://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>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2bxk

From Proteopedia

Revision as of 12:11, 27 April 2022

Human serum albumin complexed with myristate, azapropazone and indomethacin

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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