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1gnj

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Revision as of 06:40, 24 July 2019

HUMAN SERUM ALBUMIN COMPLEXED WITH cis-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)

Structural highlights

1gnj is a 1 chain structure with sequence from Human. The January 2003 RCSB PDB Molecule of the Month feature on Serum Albumin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1ao6, 1bj5, 1bke, 1bm0, 1e78, 1e7a, 1e7b, 1e7c, 1e7e, 1e7f, 1e7g, 1e7h, 1e7i, 1h9z, 1ha2, 1gni, 1uor
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The primary ligands of human serum albumin (HSA), an abundant plasma protein, are non-esterified fatty acids. In vivo, the majority of fatty acids associated with the protein are unsaturated. We present here the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid (C18:1) and the polyunsaturated arachidonic acid (C20:4). Both compounds are observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids. Although C18:1 fatty acid binds each site on HSA in a conformation almost identical with that of the corresponding saturated compound (C18:0), the presence of multiple cis double bonds in C20:4 induces distinct binding configurations at some sites. The observed restriction on binding configurations plausibly accounts for differences in the pattern of binding affinities for the primary sites between polyunsaturated fatty acids and their saturated or monounsaturated counterparts.

Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids.,Petitpas I, Grune T, Bhattacharya AA, Curry S J Mol Biol. 2001 Dec 14;314(5):955-60. PMID:11743713^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Petitpas I, Grune T, Bhattacharya AA, Curry S. Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. PMID:11743713 doi:http://dx.doi.org/10.1006/jmbi.2000.5208

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gnj"

@@ Line 1: / Line 1: @@
 ==HUMAN SERUM ALBUMIN COMPLEXED WITH cis-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)==
-<StructureSection load='1gnj' size='340' side='right' caption='[[1gnj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='1gnj' size='340' side='right'caption='[[1gnj]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1gnj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The January 2003 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Serum Albumin''  by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2003_1 10.2210/rcsb_pdb/mom_2003_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GNJ FirstGlance]. <br>
@@ Line 31: / Line 31: @@
 </div>
 <div class="pdbe-citations 1gnj" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Albumin 3D structures|Albumin 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 39: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: RCSB PDB Molecule of the Month]]
 [[Category: Serum Albumin]]

1gnj

From Proteopedia

Revision as of 06:40, 24 July 2019

HUMAN SERUM ALBUMIN COMPLEXED WITH cis-5,8,11,14-EICOSATETRAENOIC ACID (ARACHIDONIC ACID)

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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