3b9m: Difference between revisions
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{{STRUCTURE_3b9m| PDB=3b9m | SCENE= }} | {{STRUCTURE_3b9m| PDB=3b9m | SCENE= }} | ||
===Human serum albumin complexed with myristate, 3'-azido-3'-deoxythymidine (AZT) and salicylic acid=== | |||
{{ABSTRACT_PUBMED_18258455}} | |||
=== | ==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> | |||
==About this Structure== | ==About this Structure== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:018258455</ref><ref group="xtra">PMID:016169013</ref><ref group="xtra">PMID:017067818</ref><ref group="xtra">PMID:001630489</ref><references group="xtra"/> | <ref group="xtra">PMID:018258455</ref><ref group="xtra">PMID:016169013</ref><ref group="xtra">PMID:017067818</ref><ref group="xtra">PMID:001630489</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
Revision as of 00:41, 25 March 2013
Human serum albumin complexed with myristate, 3'-azido-3'-deoxythymidine (AZT) and salicylic acidHuman serum albumin complexed with myristate, 3'-azido-3'-deoxythymidine (AZT) and salicylic acid
Template:ABSTRACT PUBMED 18258455
DiseaseDisease
[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]
FunctionFunction
[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 StructureAbout this Structure
3b9m is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
[xtra 1][xtra 2][xtra 3][xtra 4]
- ↑ Zhu L, Yang F, Chen L, Meehan EJ, Huang M. A new drug binding subsite on human serum albumin and drug-drug interaction studied by X-ray crystallography. J Struct Biol. 2008 Apr;162(1):40-9. Epub 2007 Dec 28. PMID:18258455 doi:10.1016/j.jsb.2007.12.004
- ↑ Ghuman J, Zunszain PA, Petitpas I, Bhattacharya AA, Otagiri M, Curry S. Structural basis of the drug-binding specificity of human serum albumin. J Mol Biol. 2005 Oct 14;353(1):38-52. PMID:16169013 doi:http://dx.doi.org/10.1016/j.jmb.2005.07.075
- ↑ Yang F, Bian C, Zhu L, Zhao G, Huang Z, Huang M. Effect of human serum albumin on drug metabolism: structural evidence of esterase activity of human serum albumin. J Struct Biol. 2007 Feb;157(2):348-55. Epub 2006 Sep 9. PMID:17067818 doi:10.1016/j.jsb.2006.08.015
- ↑ He XM, Carter DC. Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15. PMID:1630489 doi:http://dx.doi.org/10.1038/358209a0
- ↑ 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