Angiotensin II is bound to both receptors AT<sub>1</sub>and AT<sub>2</sub>, parallel to the transmembrane domains and in an extended form

Deraët, Maud; Řihakova, Lenka; Boucard, Antony A.; Pérodin, Jacqueline; Sauvé, Simon; Mathieu, Axel; Guillemette, Gaétan; Leduc, Richard; Lavigne, Pierre; Escher, Emanuel

doi:10.1139/y02-060

Cited by 26 publications

(40 citation statements)

References 22 publications

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“…All the calculations were performed on an SGI Octane2 workstation (Silicon Graphics Inc., Mountain View, CA), as described previously (36). Briefly, a pairwise sequence alignment between the primary structures of BLT1 (SwissProt accession no.…”

Section: Methodsmentioning

confidence: 99%

“…D89078) and the bovine rhodopsin (Protein Data Bank: 1L9H) was performed using the program HOMOLOGY. The sequences of the two proteins were aligned so as to match the positions of the following conserved residues: Asn 55 -Asn1.50 36 (the superscripts represent the residue numbering in rhodopsin structure Protein Data Bank code 1F88, and human BLT1 sequence, respectively, and 1.50 is the numbering in the standardized nomenclature), Asp 83 -Asp2.50 64 282 . The coordinates of the identified structurally conserved regions were then transferred to the sequence of the BLT1.…”

Section: Methodsmentioning

confidence: 99%

“…Modeling of the BLT1 Structure on the Bovine Rhopdosin Model-The homology model of the BLT1 was based on the crystal structure of bovine rhodopsin and was obtained as described elsewhere (36). In our model, it can be seen that the two dileucine motifs are located within helix VIII and that the distal motif is involved in an hydrophobic core containing other hydrophobic residues in helix VIII (of which the strictly conserved Phe 313 -Phe7.60 300 ) and in helix I.…”

Section: Table III Internalization Levels Of Wt and Mutant Blt1mentioning

confidence: 99%

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Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Gaudreau¹,

Beaulieu

Chen³

et al. 2004

Journal of Biological Chemistry

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Mutational analysis of determinants located in the C-terminal (C) tail of the high affinity leukotriene (LT)BA variety of stimuli, including light, neurotransmitters, hormones, and inflammatory lipid mediators produce their effects via activation of G-protein-coupled receptors (GPCRs). 1 Taking into account the heterogeneity of ligands, it is interesting that all members of this superfamily of receptors share the same topology characterized by the presence of seven transmembrane ␣-helices. Conserved residues within subfamily A (related to rhodopsin) are localized throughout these helices, serving as reference points for sequence alignments. Biophysical and biochemical evidence indicate that upon photoactivation, relative movements of transmembrane (TM) 3 and TM6 occur in rhodopsin; similarly, rearrangement of the cytoplasmic proximal portion of TM7 relative to TM1 and of TM2 relative to the intracellular helix VIII were also observed (reviewed in Ref.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Table III Internalization Levels Of Wt and Mutant Blt1mentioning

confidence: 99%

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Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Gaudreau¹,

Beaulieu

Chen³

et al. 2004

Journal of Biological Chemistry

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“…1 Ang II is an octapeptide hormone (Asp1-Arg2-Val3-Tyr4-Ile5-His6-Pro7-Phe8, DRVYIHPF) that has been studied for several decades in the structure-dependent activity of the biological pathway of the Ang II receptor. [2][3][4][5][6][7][8][9][10][11][12][13] Free Ang II molecular structures in solutions have been investigated with a variety of techniques. The results have been reported as β-turn, random coil, hair-pin and other structures.…”

mentioning

confidence: 99%

Determination of a Binding Site of Cu, Ni, Mg, and Ca Metal Ions with Angiotensin II Peptide by Electrospray Tandem Mass Spectrometry

Kim¹,

Kim²,

Kim³

2010

Bulletin of the Korean Chemical Society

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Angiotensin II (Ang II) is the main active hormone in the renin-angiotensin blood pressure regulation system. 1 Ang II is an octapeptide hormone (Asp1-Arg2-Val3-Tyr4-Ile5-His6-Pro7-Phe8, DRVYIHPF) that has been studied for several decades in the structure-dependent activity of the biological pathway of the Ang II receptor. [2][3][4][5][6][7][8][9][10][11][12][13] Free Ang II molecular structures in solutions have been investigated with a variety of techniques. The results have been reported as β-turn, random coil, hair-pin and other structures.2-8 The structures of Ang II complexed with a receptor have been reported as a hair-pin or an extended structure in NMR and crystallography studies. [9][10][11][12][13] It is evident that several reports are not consistent with each other and that no clear agreement exists regarding the biologically active structure of Ang II during the biological process.For the study of blood pressure control and metal-peptide interaction, the influences of metal cations on the biological activity of Ang II have been also investigated. , and Ca 2+ ) and the Ang II molecule to explain the biological effect in terms of a gas-phase structural difference. We present the results of a tandem mass spectrometry and multiple mass spectrometry study regarding the interaction of metal ions with the Ang II molecule, the C-terminus amidated Ang II molecule (DRVYIHPF-NH 2 ), and two of its segments: the N-terminus tetrapeptide Asp1-Arg2-Val3-Tyr4-NH2 (DRVY-NH2) and the N-terminus hexapeptide Asp1-Arg2-Val3-Tyr4-Ile5-His6-NH2 (DRVYIH-NH2). Two N-terminus segments are used to confirm the [metal II + Ang II] 2+ complex formation efficiency and the metal binding site. Experimental SectionThe gas-phase [metal II + Ang II] 2+ cation complexes were produced by an electrospray ionization source. The experimental MS/MS and MS/MS/MS spectra for fragmentation pattern analysis were obtained using a Thermo Finnigan LTQ mass spectrometer (Thermo Electron Corp., San Jose, CA, USA). This mass spectrometer is a linear ion trap mass spectrometer equipped with an atmospheric pressure-ionization source. LTQ conditions. The samples were introduced into the electrospray interface by a direct infusion method using a microsyringe pump (SGE, Australia) at a flow rate of 5 µL min. The MS/MS spectra were acquired with experimental conditions of an isolation width of 0.5 -1 mass unit, an activation time of 30 msec and q z = 0.25. In MS/MS or MS/MS/MS mode, the parent ion molecules were manually selected one by one, and each was subjected to collision-induced dissociation (CID).Reagents. Ang II human (96%, Fluka), DRVYIHPF-NH2 (> 90%, Peptron, Daejeon, Korea), DRVY-NH2 (> 90%, Peptron, Daejeon, Korea), DRVYIH-NH2 (> 90%, Peptron, Daejeon, Korea), CuCl 2 ․2H 2 O (99%, Sigma-Aldrich Korea), Ni(NO 5 ) 2 ․ 6H2O (97%, Junsei chemical Co., Tokyo, Japan), CaCl2․2H2O (98%, Daejung Chemical Korea), Mg(NO3)2․6H2O (98%, Junsei chemical Co., Tokyo, Japan), and H2O (HPLC grade, Merck) were used in experiments. Ang II was dissolved in water to...

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“…[1][2][3][4] Metal ion influences on the biological activity of Ang II have also been investigated. [5][6][7][8][9][10][11][12][13][14] Blood pressure was observed to increase as a result of the influence of Li, Na, Mg, and Ca ions on the renin-angiotensin system.…”

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confidence: 99%

DFT Study of the [Cu-Angiotensin II]²⁺Complex Structure

Kim¹,

Kim²

2012

Bulletin of the Korean Chemical Society

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Angiotensin II is bound to both receptors AT₁and AT₂, parallel to the transmembrane domains and in an extended form

Cited by 26 publications

References 22 publications

Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Determination of a Binding Site of Cu, Ni, Mg, and Ca Metal Ions with Angiotensin II Peptide by Electrospray Tandem Mass Spectrometry

DFT Study of the [Cu-Angiotensin II]²⁺Complex Structure

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Angiotensin II is bound to both receptors AT1and AT2, parallel to the transmembrane domains and in an extended form

Cited by 26 publications

References 22 publications

Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Structural Determinants Regulating Expression of the High Affinity Leukotriene B4 Receptor

Determination of a Binding Site of Cu, Ni, Mg, and Ca Metal Ions with Angiotensin II Peptide by Electrospray Tandem Mass Spectrometry

DFT Study of the [Cu-Angiotensin II]2+Complex Structure

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Angiotensin II is bound to both receptors AT₁and AT₂, parallel to the transmembrane domains and in an extended form

DFT Study of the [Cu-Angiotensin II]²⁺Complex Structure