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2xvv

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Revision as of 12:18, 27 April 2022

Human serum albumin complexed with dansyl-L-asparagine and myristic acid

Structural highlights

2xvv 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:	2bxq, 1hk4, 2xvu, 2bxi, 2vuf, 1o9x, 1bke, 2bxk, 1hk1, 1uor, 1h9z, 1e7b, 1hk2, 1hk5, 2esg, 1e7e, 2bxg, 2xvq, 2bxh, 2bxo, 2bxf, 1ysx, 1e7g, 1ao6, 2bxc, 2bxe, 1tf0, 2bxn, 1e7c, 1gnj, 1e7h, 2xw0, 2bxa, 1hk3, 2xsi, 2xvw, 2bxb, 1e7i, 2xw1, 2bxl, 1gni, 1ha2, 1bj5, 1e7a, 2bxp, 2bxd, 1bm0, 1e78, 2vdb, 1e7f, 1n5u, 2bxm, 2bx8, 2vue
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

Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.

Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin.,Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S J Struct Biol. 2010 Oct 18. PMID:20940056^[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
↑ Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004

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/2xvv"

Categories: Human | Large Structures | Curry, S | Ghuman, J | Transport protein

@@ Line 3: / Line 3: @@
 <StructureSection load='2xvv' size='340' side='right'caption='[[2xvv]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xvv]] 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=2XVV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XVV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2xvv]] 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=2XVV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVV FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9DN:DANSYL-L-ASPARAGINE'>9DN</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">[[2bxq|2bxq]], [[1hk4|1hk4]], [[2xvu|2xvu]], [[2bxi|2bxi]], [[2vuf|2vuf]], [[1o9x|1o9x]], [[1bke|1bke]], [[2bxk|2bxk]], [[1hk1|1hk1]], [[1uor|1uor]], [[1h9z|1h9z]], [[1e7b|1e7b]], [[1hk2|1hk2]], [[1hk5|1hk5]], [[2esg|2esg]], [[1e7e|1e7e]], [[2bxg|2bxg]], [[2xvq|2xvq]], [[2bxh|2bxh]], [[2bxo|2bxo]], [[2bxf|2bxf]], [[1ysx|1ysx]], [[1e7g|1e7g]], [[1ao6|1ao6]], [[2bxc|2bxc]], [[2bxe|2bxe]], [[1tf0|1tf0]], [[2bxn|2bxn]], [[1e7c|1e7c]], [[1gnj|1gnj]], [[1e7h|1e7h]], [[2xw0|2xw0]], [[2bxa|2bxa]], [[1hk3|1hk3]], [[2xsi|2xsi]], [[2xvw|2xvw]], [[2bxb|2bxb]], [[1e7i|1e7i]], [[2xw1|2xw1]], [[2bxl|2bxl]], [[1gni|1gni]], [[1ha2|1ha2]], [[1bj5|1bj5]], [[1e7a|1e7a]], [[2bxp|2bxp]], [[2bxd|2bxd]], [[1bm0|1bm0]], [[1e78|1e78]], [[2vdb|2vdb]], [[1e7f|1e7f]], [[1n5u|1n5u]], [[2bxm|2bxm]], [[2bx8|2bx8]], [[2vue|2vue]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bxq|2bxq]], [[1hk4|1hk4]], [[2xvu|2xvu]], [[2bxi|2bxi]], [[2vuf|2vuf]], [[1o9x|1o9x]], [[1bke|1bke]], [[2bxk|2bxk]], [[1hk1|1hk1]], [[1uor|1uor]], [[1h9z|1h9z]], [[1e7b|1e7b]], [[1hk2|1hk2]], [[1hk5|1hk5]], [[2esg|2esg]], [[1e7e|1e7e]], [[2bxg|2bxg]], [[2xvq|2xvq]], [[2bxh|2bxh]], [[2bxo|2bxo]], [[2bxf|2bxf]], [[1ysx|1ysx]], [[1e7g|1e7g]], [[1ao6|1ao6]], [[2bxc|2bxc]], [[2bxe|2bxe]], [[1tf0|1tf0]], [[2bxn|2bxn]], [[1e7c|1e7c]], [[1gnj|1gnj]], [[1e7h|1e7h]], [[2xw0|2xw0]], [[2bxa|2bxa]], [[1hk3|1hk3]], [[2xsi|2xsi]], [[2xvw|2xvw]], [[2bxb|2bxb]], [[1e7i|1e7i]], [[2xw1|2xw1]], [[2bxl|2bxl]], [[1gni|1gni]], [[1ha2|1ha2]], [[1bj5|1bj5]], [[1e7a|1e7a]], [[2bxp|2bxp]], [[2bxd|2bxd]], [[1bm0|1bm0]], [[1e78|1e78]], [[2vdb|2vdb]], [[1e7f|1e7f]], [[1n5u|1n5u]], [[2bxm|2bxm]], [[2bx8|2bx8]], [[2vue|2vue]]</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=2xvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvv OCA], [http://pdbe.org/2xvv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xvv RCSB], [http://www.ebi.ac.uk/pdbsum/2xvv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvv 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=2xvv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvv OCA], [https://pdbe.org/2xvv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xvv RCSB], [https://www.ebi.ac.uk/pdbsum/2xvv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvv 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2xvv

From Proteopedia

Revision as of 12:18, 27 April 2022

Human serum albumin complexed with dansyl-L-asparagine and myristic acid

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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