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==Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function Relationship==
The line below this paragraph, containing "STRUCTURE_1n9u", creates the "Structure Box" on the page.
<StructureSection load='1n9u' size='340' side='right'caption='[[1n9u]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1n9u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9U FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-->
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9u OCA], [https://pdbe.org/1n9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9u RCSB], [https://www.ebi.ac.uk/pdbsum/1n9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9u ProSAT]</span></td></tr>
{{STRUCTURE_1n9u|  PDB=1n9u  |  SCENE=  }}
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ANGT_HUMAN ANGT_HUMAN] Genetic variations in AGT are a cause of susceptibility to essential hypertension (EHT) [MIM:[https://omim.org/entry/145500 145500]. Essential hypertension is a condition in which blood pressure is consistently higher than normal with no identifiable cause.  Defects in AGT are a cause of renal tubular dysgenesis (RTD) [MIM:[https://omim.org/entry/267430 267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).<ref>PMID:16116425</ref>
== Function ==
[https://www.uniprot.org/uniprot/ANGT_HUMAN ANGT_HUMAN] Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.<ref>PMID:1132082</ref> <ref>PMID:10619573</ref> <ref>PMID:17138938</ref>  Angiotensin-2: acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone.<ref>PMID:1132082</ref> <ref>PMID:10619573</ref> <ref>PMID:17138938</ref>  Angiotensin-3: stimulates aldosterone release.<ref>PMID:1132082</ref> <ref>PMID:10619573</ref> <ref>PMID:17138938</ref>  Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity).<ref>PMID:1132082</ref> <ref>PMID:10619573</ref> <ref>PMID:17138938</ref>  


'''Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Strucure-Function Relationship'''
==See Also==
 
*[[Angiotensin-Converting Enzyme|Angiotensin-Converting Enzyme]]
 
== References ==
==Overview==
<references/>
Conformational analysis of angiotensin I (AI) and II (AII) peptides has been performed through 2D 1H-NMR spectroscopy in dimethylsulfoxide and 2,2,2-trifluoroethanol/H2O. The solution structural models of AI and AII have been determined in dimethylsulfoxide using NOE distance and 3JHNHalpha coupling constants. Finally, the AI family of models resulting from restrained energy minimization (REM) refinement, exhibits pairwise rmsd values for the family ensemble 0.26 +/- 0.13 A, 1.05 +/- 0.23 A, for backbone and heavy atoms, respectively, and the distance penalty function is calculated at 0.075 +/- 0.006 A2. Comparable results have been afforded for AII ensemble (rmsd values 0.30 +/- 0.22 A, 1.38 +/- 0.48 A for backbone and heavy atoms, respectively; distance penalty function is 0.029 +/- 0.003 A2). The two peptides demonstrate similar N-terminal and different C-terminal conformation as a consequence of the presence/absence of the His9-Leu10 dipeptide, which plays an important role in the different biological function of the two peptides. Other conformational variations focused on the side-chain orientation of aromatic residues, which constitute a biologically relevant hydrophobic core and whose inter-residue contacts are strong in dimethylsulfoxide and are retained even in mixed organic-aqueous media. Detailed analysis of the peptide structural features attempts to elucidate the conformational role of the C-terminal dipeptide to the different binding affinity of AI and AII towards the AT1 receptor and sets the basis for understanding the factors that might govern free- or bound-depended AII structural differentiation.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Homo sapiens]]
1N9U is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9U OCA].
[[Category: Large Structures]]
 
[[Category: Cordopatis P]]
==Reference==
[[Category: Gerothanassis IP]]
Comparison of the solution structures of angiotensin I &amp; II. Implication for structure-function relationship., Spyroulias GA, Nikolakopoulou P, Tzakos A, Gerothanassis IP, Magafa V, Manessi-Zoupa E, Cordopatis P, Eur J Biochem. 2003 May;270(10):2163-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12752436 12752436]
[[Category: Magafa V]]
[[Category: Single protein]]
[[Category: Manessi-Zoupa E]]
[[Category: Cordopatis, P.]]
[[Category: Nikolakopoulou P]]
[[Category: Gerothanassis, I P.]]
[[Category: Spyroulias GA]]
[[Category: Magafa, V.]]
[[Category: Tzakos A]]
[[Category: Manessi-Zoupa, E.]]
[[Category: Nikolakopoulou, P.]]
[[Category: Spyroulias, G A.]]
[[Category: Tzakos, A.]]
[[Category: Angiotensin]]
[[Category: Nmr solution structure]]
[[Category: Peptide]]
[[Category: Renin-angiotensin system]]
[[Category: Solid phase peptide synthesis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:16:18 2008''

Latest revision as of 09:32, 1 May 2024

Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function RelationshipDifferences and Similarities in Solution Structures of Angiotensin I & II: Implication for Structure-Function Relationship

Structural highlights

1n9u is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ANGT_HUMAN Genetic variations in AGT are a cause of susceptibility to essential hypertension (EHT) [MIM:145500. Essential hypertension is a condition in which blood pressure is consistently higher than normal with no identifiable cause. Defects in AGT are a cause of renal tubular dysgenesis (RTD) [MIM:267430. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).[1]

Function

ANGT_HUMAN Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.[2] [3] [4] Angiotensin-2: acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone.[5] [6] [7] Angiotensin-3: stimulates aldosterone release.[8] [9] [10] Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity).[11] [12] [13]

See Also

References

  1. ↑ Gribouval O, Gonzales M, Neuhaus T, Aziza J, Bieth E, Laurent N, Bouton JM, Feuillet F, Makni S, Ben Amar H, Laube G, Delezoide AL, Bouvier R, Dijoud F, Ollagnon-Roman E, Roume J, Joubert M, Antignac C, Gubler MC. Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet. 2005 Sep;37(9):964-8. Epub 2005 Aug 14. PMID:16116425 doi:ng1623
  2. ↑ Goodfriend TL, Peach MJ. Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. PMID:1132082
  3. ↑ Weir MR, Dzau VJ. The renin-angiotensin-aldosterone system: a specific target for hypertension management. Am J Hypertens. 1999 Dec;12(12 Pt 3):205S-213S. PMID:10619573
  4. ↑ Jankowski V, Vanholder R, van der Giet M, Tolle M, Karadogan S, Gobom J, Furkert J, Oksche A, Krause E, Tran TN, Tepel M, Schuchardt M, Schluter H, Wiedon A, Beyermann M, Bader M, Todiras M, Zidek W, Jankowski J. Mass-spectrometric identification of a novel angiotensin peptide in human plasma. Arterioscler Thromb Vasc Biol. 2007 Feb;27(2):297-302. Epub 2006 Nov 30. PMID:17138938 doi:10.1161/01.ATV.0000253889.09765.5f
  5. ↑ Goodfriend TL, Peach MJ. Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. PMID:1132082
  6. ↑ Weir MR, Dzau VJ. The renin-angiotensin-aldosterone system: a specific target for hypertension management. Am J Hypertens. 1999 Dec;12(12 Pt 3):205S-213S. PMID:10619573
  7. ↑ Jankowski V, Vanholder R, van der Giet M, Tolle M, Karadogan S, Gobom J, Furkert J, Oksche A, Krause E, Tran TN, Tepel M, Schuchardt M, Schluter H, Wiedon A, Beyermann M, Bader M, Todiras M, Zidek W, Jankowski J. Mass-spectrometric identification of a novel angiotensin peptide in human plasma. Arterioscler Thromb Vasc Biol. 2007 Feb;27(2):297-302. Epub 2006 Nov 30. PMID:17138938 doi:10.1161/01.ATV.0000253889.09765.5f
  8. ↑ Goodfriend TL, Peach MJ. Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. PMID:1132082
  9. ↑ Weir MR, Dzau VJ. The renin-angiotensin-aldosterone system: a specific target for hypertension management. Am J Hypertens. 1999 Dec;12(12 Pt 3):205S-213S. PMID:10619573
  10. ↑ Jankowski V, Vanholder R, van der Giet M, Tolle M, Karadogan S, Gobom J, Furkert J, Oksche A, Krause E, Tran TN, Tepel M, Schuchardt M, Schluter H, Wiedon A, Beyermann M, Bader M, Todiras M, Zidek W, Jankowski J. Mass-spectrometric identification of a novel angiotensin peptide in human plasma. Arterioscler Thromb Vasc Biol. 2007 Feb;27(2):297-302. Epub 2006 Nov 30. PMID:17138938 doi:10.1161/01.ATV.0000253889.09765.5f
  11. ↑ Goodfriend TL, Peach MJ. Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system. Circ Res. 1975 Jun;36(6 Suppl 1):38-48. PMID:1132082
  12. ↑ Weir MR, Dzau VJ. The renin-angiotensin-aldosterone system: a specific target for hypertension management. Am J Hypertens. 1999 Dec;12(12 Pt 3):205S-213S. PMID:10619573
  13. ↑ Jankowski V, Vanholder R, van der Giet M, Tolle M, Karadogan S, Gobom J, Furkert J, Oksche A, Krause E, Tran TN, Tepel M, Schuchardt M, Schluter H, Wiedon A, Beyermann M, Bader M, Todiras M, Zidek W, Jankowski J. Mass-spectrometric identification of a novel angiotensin peptide in human plasma. Arterioscler Thromb Vasc Biol. 2007 Feb;27(2):297-302. Epub 2006 Nov 30. PMID:17138938 doi:10.1161/01.ATV.0000253889.09765.5f
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