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2xvq

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Revision as of 07:47, 24 July 2019

Human serum albumin complexed with dansyl-L-sarcosine

Structural highlights

2xvq is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2bxq, 1hk4, 2bxi, 2vuf, 1o9x, 1bke, 2bxk, 1hk1, 1uor, 1e7b, 1h9z, 1hk2, 2esg, 1hk5, 1e7e, 2bxg, 2bxh, 2bxo, 2bxf, 1ysx, 1e7g, 1tf0, 2bxn, 2bxe, 2bxc, 1ao6, 1e7c, 1gnj, 1e7h, 2bxa, 1hk3, 2bxb, 1e7i, 2bxl, 1gni, 1ha2, 1bj5, 1e7a, 2bxp, 2bxd, 1e78, 1bm0, 2vdb, 1e7f, 1n5u, 2bx8, 2bxm, 2vue, 2xvw, 2xvu, 2xvv, 2xw0, 2xsi, 2xw1
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]

Publication Abstract from PubMed

Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.

Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin.,Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S J Struct Biol. 2010 Oct 18. PMID:20940056^[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
↑ Ryan AJ, Ghuman J, Zunszain PA, Chung CW, Curry S. Structural basis of binding of fluorescent, site-specific dansylated amino acids to human serum albumin. J Struct Biol. 2010 Oct 18. PMID:20940056 doi:10.1016/j.jsb.2010.10.004

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xvq"

Categories: Human | Large Structures | Curry, S | Ryan, A J | Transport protein

@@ Line 1: / Line 1: @@
 ==Human serum albumin complexed with dansyl-L-sarcosine==
-<StructureSection load='2xvq' size='340' side='right' caption='[[2xvq]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='2xvq' size='340' side='right'caption='[[2xvq]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2xvq]] is a 2 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=2XVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XVQ FirstGlance]. <br>
@@ Line 23: / Line 23: @@
 ==See Also==
-*[[Albumin|Albumin]]
+*[[Albumin 3D structures|Albumin 3D structures]]
 == References ==
 <references/>
@@ Line 29: / Line 29: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Curry, S]]
 [[Category: Ryan, A J]]
 [[Category: Transport protein]]

2xvq

From Proteopedia

Revision as of 07:47, 24 July 2019

Human serum albumin complexed with dansyl-L-sarcosine

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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