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2vdb

From Proteopedia

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Structure of human serum albumin with S-naproxen and the GA module

Structural highlights

2vdb is a 2 chain structure with sequence from Finegoldia magna and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.52Å
Ligands:	,
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

The previously determined crystal structure of the bacterial albumin-binding GA module in complex with human serum albumin (HSA) suggested the possibility of utilizing the complex in the study of ligand binding to HSA. As a continuation of these studies, the crystal structure of the HSA-GA complex with the drug molecule naproxen and the fatty acid decanoate bound to HSA has been determined to a resolution of 2.5 A. In terms of drug binding, the structure suggests that the binding of decanoate to the albumin molecule may play a role in making the haemin site in subdomain IB of the albumin molecule available for the binding of naproxen. In addition, structure comparisons with solved structures of HSA and of the HSA-GA complex show that the GA module is capable of binding to different conformations of HSA. The HSA-GA complex therefore emerges as a possible platform for the crystallographic study of specific HSA-drug interactions and of the influence exerted by the presence of fatty acids.

Structural basis for the binding of naproxen to human serum albumin in the presence of fatty acids and the GA module.,Lejon S, Cramer JF, Nordberg P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt, 2):64-9. Epub 2008 Jan 18. PMID:18259051^[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
↑ Lejon S, Cramer JF, Nordberg P. Structural basis for the binding of naproxen to human serum albumin in the presence of fatty acids and the GA module. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt, 2):64-9. Epub 2008 Jan 18. PMID:18259051 doi:http://dx.doi.org/10.1107/S174430910706770X

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/2vdb"

@@ Line 1: / Line 1: @@
-==STRUCTURE OF HUMAN SERUM ALBUMIN WITH S-NAPROXEN AND THE GA MODULE==
-<StructureSection load='2vdb' size='340' side='right' caption='[[2vdb]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
+==Structure of human serum albumin with S-naproxen and the GA module==
+<StructureSection load='2vdb' size='340' side='right'caption='[[2vdb]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vdb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vdb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VDB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</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]] 2.52&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bm0|1bm0]], [[1e7a|1e7a]], [[1e7e|1e7e]], [[1e7g|1e7g]], [[1gni|1gni]], [[1h9z|1h9z]], [[1ha2|1ha2]], [[1hk1|1hk1]], [[1hk4|1hk4]], [[1hk5|1hk5]], [[1tf0|1tf0]], [[1uor|1uor]], [[1ysx|1ysx]], [[2bx8|2bx8]], [[2bxa|2bxa]], [[2bxb|2bxb]], [[2bxc|2bxc]], [[2bxd|2bxd]], [[2bxi|2bxi]], [[2bxo|2bxo]], [[2bxq|2bxq]], [[1ao6|1ao6]], [[1bj5|1bj5]], [[1bke|1bke]], [[1e78|1e78]], [[1e7b|1e7b]], [[1e7c|1e7c]], [[1e7f|1e7f]], [[1e7h|1e7h]], [[1e7i|1e7i]], [[1gnj|1gnj]], [[1hk2|1hk2]], [[1hk3|1hk3]], [[1n5u|1n5u]], [[1o9x|1o9x]], [[2bxe|2bxe]], [[2bxf|2bxf]], [[2bxg|2bxg]], [[2bxh|2bxh]], [[2bxk|2bxk]], [[2bxl|2bxl]], [[2bxm|2bxm]], [[2bxn|2bxn]], [[2bxp|2bxp]], [[2esg|2esg]], [[1gab|1gab]], [[1prb|1prb]], [[2j5y|2j5y]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=NPS:(2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC+ACID'>NPS</scene></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=2vdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vdb RCSB], [http://www.ebi.ac.uk/pdbsum/2vdb PDBsum]</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=2vdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdb OCA], [https://pdbe.org/2vdb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vdb RCSB], [https://www.ebi.ac.uk/pdbsum/2vdb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdb 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]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vdb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vdb_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vdb ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2vdb" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Albumin|Albumin]]
+*[[Albumin 3D structures|Albumin 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 40: @@
 [[Category: Finegoldia magna]]
 [[Category: Homo sapiens]]
-[[Category: Cramer, J F]]
+[[Category: Large Structures]]
-[[Category: Lejon, S]]
+[[Category: Cramer JF]]
-[[Category: Nordberg, P A]]
+[[Category: Lejon S]]
-[[Category: Bacterial albumin-binding]]
+[[Category: Nordberg PA]]
-[[Category: Cell wall]]
-[[Category: Cleavage on pair of basic residue]]
-[[Category: Disease mutation]]
-[[Category: Drug binding]]
-[[Category: Ga module]]
-[[Category: Glycation]]
-[[Category: Glycoprotein]]
-[[Category: Human serum albumin]]
-[[Category: Lipid-binding]]
-[[Category: Metal-binding]]
-[[Category: Naproxen]]
-[[Category: Peptidoglycan-anchor]]
-[[Category: Protein binding]]
-[[Category: Secreted]]
-[[Category: Three-helix bundle]]

2vdb

From Proteopedia

Current revision

Structure of human serum albumin with S-naproxen and the GA module

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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