1srb: Difference between revisions

Revision as of 16:23, 28 July 2008

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File:1srb.png

Template:STRUCTURE 1srb

CONFORMATIONAL STUDIES ON SRTB, A NON-SELECTIVE ENDOTHELIN RECEPTOR AGONIST, AND ON IRL 1620, AN ETB RECEPTOR SPECIFIC AGONISTCONFORMATIONAL STUDIES ON SRTB, A NON-SELECTIVE ENDOTHELIN RECEPTOR AGONIST, AND ON IRL 1620, AN ETB RECEPTOR SPECIFIC AGONIST

Template:ABSTRACT PUBMED 7849060

About this StructureAbout this Structure

1SRB is a Single protein structure of sequence from Atractaspis microlepidota andersoni. Full experimental information is available from OCA.

ReferenceReference

1H NMR studies of sarafotoxin SRTb, a nonselective endothelin receptor agonist, and IRL 1620, an ETB receptor-specific agonist., Atkins AR, Martin RC, Smith R, Biochemistry. 1995 Feb 14;34(6):2026-33. PMID:7849060

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

OCA

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-'''CONFORMATIONAL STUDIES ON SRTB, A NON-SELECTIVE ENDOTHELIN RECEPTOR AGONIST, AND ON IRL 1620, AN ETB RECEPTOR SPECIFIC AGONIST'''
+===CONFORMATIONAL STUDIES ON SRTB, A NON-SELECTIVE ENDOTHELIN RECEPTOR AGONIST, AND ON IRL 1620, AN ETB RECEPTOR SPECIFIC AGONIST===
-==Overview==
+<!--
-H NMR studies on the nonselective endothelin receptor agonist sarafotoxin SRTb have identified a helix between residues Asp 8 and His 16, and a beta-turn involving residues Cys 3 to Met 6; however, the biologically important C-terminal five residues were found to be conformationally variable. The average RMSD, measured for the final 43 refined structures to the average structure over residues 1-16, was 0.78 +/- 0.18 A for the backbone atoms and 1.39 +/- 0.22 A for all atoms. The torsion angles Cys 3 psi/Lys 4 theta, Thr 7 psi/Asp 8 theta and Gln 17 theta were identified as sites of conformational variability. Differences were found between the structures in the bicyclic loop region for SRTb and those published for ET1, another nonselective receptor agonist, which may explain the observed differences in potency of these peptides. The conformation of an ETB receptor-specific agonist, IRL 1620, which lacks the N-terminal seven residues and the two intrachain disulfides, was found by NMR and circular dichroism spectroscopy to be predominantly random coil, despite the fact that its affinity for the ETB receptor almost equals that of ET1. However, close analysis of the NMR results indicated the presence of turn-like structures, or a nascent helix, in the part of the sequence corresponding to the helical region in the parent peptides. These results suggest that the helical conformation may be required for ligand binding to the ETB receptor as well as to the ETA receptor.
+The line below this paragraph, {{ABSTRACT_PUBMED_7849060}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7849060 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7849060}}
 ==About this Structure==
-SRB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Atractaspis_microlepidota_andersoni Atractaspis microlepidota andersoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRB OCA].
+SRB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Atractaspis_microlepidota_andersoni Atractaspis microlepidota andersoni]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SRB OCA].
 ==Reference==
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 [[Category: Smith, R.]]
 [[Category: Toxin]]
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