1N9U

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


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 300 
  • Conformers Submitted: 21 
  • Selection Criteria: target function for models 1-20, mean energy minimized for model 21 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Comparison of the solution structures of angiotensin I & II. Implication for structure-function relationship.

Spyroulias, G.A.Nikolakopoulou, P.Tzakos, A.Gerothanassis, I.P.Magafa, V.Manessi-Zoupa, E.Cordopatis, P.

(2003) Eur J Biochem 270: 2163-2173

  • DOI: https://doi.org/10.1046/j.1432-1033.2003.03573.x
  • Primary Citation of Related Structures:  
    1N9U, 1N9V

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    Department of Pharmacy, University of Patras, Greece. G.A.Spyroulias@upatras.gr


Macromolecules

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Angiotensin I10N/AMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P01019 (Homo sapiens)
Explore P01019 
Go to UniProtKB:  P01019
PHAROS:  P01019
GTEx:  ENSG00000135744 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01019
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 300 
  • Conformers Submitted: 21 
  • Selection Criteria: target function for models 1-20, mean energy minimized for model 21 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2003-07-29
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2016-12-21
    Changes: Structure summary