1tf0
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1tf0.png|left|200px]] | ||
| - | |||
{{STRUCTURE_1tf0| PDB=1tf0 | SCENE= }} | {{STRUCTURE_1tf0| PDB=1tf0 | SCENE= }} | ||
| - | |||
===Crystal structure of the GA module complexed with human serum albumin=== | ===Crystal structure of the GA module complexed with human serum albumin=== | ||
| + | {{ABSTRACT_PUBMED_15269208}} | ||
| - | + | ==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> | ||
| + | |||
| + | ==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> [[http://www.uniprot.org/uniprot/PAB_PEPMA PAB_PEPMA]] Binds serum albumin. | ||
==About this Structure== | ==About this Structure== | ||
| - | [[1tf0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[1tf0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna_atcc_29328 Finegoldia magna atcc 29328] 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=1TF0 OCA]. |
==See Also== | ==See Also== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015269208</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015269208</ref><references group="xtra"/><references/> |
| - | [[Category: Finegoldia magna]] | + | [[Category: Finegoldia magna atcc 29328]] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Bjorck, L.]] | [[Category: Bjorck, L.]] | ||
Revision as of 12:03, 24 March 2013
Contents |
Crystal structure of the GA module complexed with human serum albumin
Template:ABSTRACT PUBMED 15269208
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] [PAB_PEPMA] Binds serum albumin.
About this Structure
1tf0 is a 2 chain structure with sequence from Finegoldia magna atcc 29328 and Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Lejon S, Frick IM, Bjorck L, Wikstrom M, Svensson S. Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin. J Biol Chem. 2004 Oct 8;279(41):42924-8. Epub 2004 Jul 21. PMID:15269208 doi:10.1074/jbc.M406957200
- ↑ 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
