4iw2

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{{STRUCTURE_4iw2| PDB=4iw2 | SCENE= }}
{{STRUCTURE_4iw2| PDB=4iw2 | SCENE= }}
===HSA-glucose complex===
===HSA-glucose complex===
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{{ABSTRACT_PUBMED_23592780}}
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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[[4iw2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IW2 OCA].
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[[4iw2]] 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=4IW2 OCA].
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==See Also==
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*[[Albumin|Albumin]]
==Reference==
==Reference==
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<references group="xtra"/><references/>
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<ref group="xtra">PMID:023592780</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Human]]
[[Category: Huang, M.]]
[[Category: Huang, M.]]
[[Category: Luo, Z.]]
[[Category: Luo, Z.]]

Revision as of 09:03, 19 March 2014

Template:STRUCTURE 4iw2

Contents

HSA-glucose complex

Template:ABSTRACT PUBMED 23592780

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

4iw2 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA.

See Also

Reference

  • Wang Y, Yu H, Shi X, Luo Z, Lin D, Huang M. Structural mechanism of ring-opening reaction of glucose by human serum albumin. J Biol Chem. 2013 May 31;288(22):15980-7. doi: 10.1074/jbc.M113.467027. Epub 2013, Apr 16. PMID:23592780 doi:http://dx.doi.org/10.1074/jbc.M113.467027
  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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