1n9v: Difference between revisions

Revision as of 07:14, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n9v.png

Template:STRUCTURE 1n9v

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

Template:ABSTRACT PUBMED 12752436

About this StructureAbout this Structure

1N9V is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Comparison of the solution structures of angiotensin I & 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:12752436

Page seeded by OCA on Tue Jul 29 07:14:18 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1n9v.gif|left|200px]]
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 {{STRUCTURE_1n9v|  PDB=1n9v  |  SCENE=  }}
-'''Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Strucure-Function Relationship.'''
+===Differences and Similarities in Solution Structures of Angiotensin I & II: Implication for Strucure-Function Relationship.===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12752436}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12752436 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12752436}}
 ==About this Structure==
-N9V is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9V OCA].
+N9V is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9V OCA].
 ==Reference==
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 [[Category: Renin-angiotensin system]]
 [[Category: Solid phase peptide synthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:16:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:14:18 2008''