4hgk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
{{STRUCTURE_4hgk| PDB=4hgk | SCENE= }}
{{STRUCTURE_4hgk| PDB=4hgk | SCENE= }}
===Shark IgNAR variable domain===
===Shark IgNAR variable domain===
 +
{{ABSTRACT_PUBMED_23632026}}
==Disease==
==Disease==
Line 12: Line 13:
==Reference==
==Reference==
-
<references group="xtra"/><references/>
+
<ref group="xtra">PMID:023632026</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Squalus acanthias]]
[[Category: Squalus acanthias]]

Revision as of 15:16, 19 June 2013

Template:STRUCTURE 4hgk

Contents

Shark IgNAR variable domain

Template:ABSTRACT PUBMED 23632026

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

4hgk is a 4 chain structure with sequence from Homo sapiens and Squalus acanthias. Full crystallographic information is available from OCA.

Reference

  • Kovalenko OV, Olland A, Piche-Nicholas N, Godbole A, King D, Svenson K, Calabro V, Muller MR, Barelle CJ, Somers W, Gill DS, Mosyak L, Tchistiakova L. Atypical Antigen Recognition Mode of a Shark IgNAR Variable Domain Characterized by Humanization and Structural Analysis. J Biol Chem. 2013 Apr 30. PMID:23632026 doi:10.1074/jbc.M112.435289
  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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4hgk"
Personal tools