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2vdb

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[[Image:2vdb.png|left|200px]]
 
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{{STRUCTURE_2vdb| PDB=2vdb | SCENE= }}
{{STRUCTURE_2vdb| PDB=2vdb | SCENE= }}
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===STRUCTURE OF HUMAN SERUM ALBUMIN WITH S-NAPROXEN AND THE GA MODULE===
===STRUCTURE OF HUMAN SERUM ALBUMIN WITH S-NAPROXEN AND THE GA MODULE===
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{{ABSTRACT_PUBMED_18259051}}
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{{ABSTRACT_PUBMED_18259051}}
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==Disease==
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[[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>
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==Function==
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[[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>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:018259051</ref><references group="xtra"/>
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<ref group="xtra">PMID:018259051</ref><references group="xtra"/><references/>
[[Category: Finegoldia magna]]
[[Category: Finegoldia magna]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 01:23, 25 March 2013

Template:STRUCTURE 2vdb

Contents

STRUCTURE OF HUMAN SERUM ALBUMIN WITH S-NAPROXEN AND THE GA MODULE

Template:ABSTRACT PUBMED 18259051

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]

About this Structure

2vdb is a 2 chain structure with sequence from Finegoldia magna and Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • 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. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

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