This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1a13

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:31, 22 November 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1a13.gif|left|200px]]
 
-
<!--
+
==G PROTEIN-BOUND CONFORMATION OF MASTOPARAN-X, NMR, 14 STRUCTURES==
-
The line below this paragraph, containing "STRUCTURE_1a13", creates the "Structure Box" on the page.
+
<StructureSection load='1a13' size='340' side='right'caption='[[1a13]]' 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'>[[1a13]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vespa_simillima_xanthoptera Vespa simillima xanthoptera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A13 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
-
{{STRUCTURE_1a13| PDB=1a13 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a13 OCA], [https://pdbe.org/1a13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a13 RCSB], [https://www.ebi.ac.uk/pdbsum/1a13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a13 ProSAT]</span></td></tr>
-
 
+
</table>
-
'''G PROTEIN-BOUND CONFORMATION OF MASTOPARAN-X, NMR, 14 STRUCTURES'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/MAST_VESXA MAST_VESXA] Mast cell degranulating peptide. Activates G proteins that couple to phospholipase C.
-
 
+
<div style="background-color:#fffaf0;">
-
==Overview==
+
== Publication Abstract from PubMed ==
Mastoparans, a family of tetradecapeptides from wasp venom, have been used as convenient low molecular weight models of receptors coupled to GTP-binding regulatory proteins (G proteins) for the understanding of the interaction between G proteins and receptors. Sukumar and Higashijima have analyzed the conformation of mastoparan-X (MP-X) bound to the G protein alpha-subunit using proton two-dimensional transferred nuclear Overhauser effect (TRNOE) spectroscopy [Sukumar, M., and Higashijima, T. (1992) J. Biol. Chem., 267, 21421-21424]. The resultant structure, however, was not well-defined due to severe overlap of peptide proton resonances. To determine the G protein-bound conformation of MP-X in detail, we have analyzed this interaction by heteronuclear multidimensional TRNOE experiments of MP-X uniformly enriched with 15N and/or 13C. By solving the overlap problem, we were able to determine the precise conformation of MP-X bound to Gi1alpha: the peptide adopts an amphiphilic alpha-helix from Trp3 to C-terminal Leu14, and the atomic root-mean-square deviation (rmsd) values in this portion about the averaged coordinates were 0.27 +/- 0.07 A for the backbone atoms (N, Calpha, C') and 0.84 +/- 0.16 A for all heavy atoms. These values are much smaller than the corresponding rmsd values of the structures obtained from the proton 2D TRNOE spectrum alone: 1.70 +/- 0.41 A for the backbone atoms (N, Calpha, C') and 2.84 +/- 0.51 A for all heavy atoms. Our results indicate that the heteronuclear multidimensional TRNOE experiments of peptides uniformly enriched with stable isotopes are a very powerful tool for analyzing the conformation of short peptides bound to large proteins. We will also discuss the structure-activity relationships of mastoparans in activating G proteins on the basis of the precise structure of MP-X bound to Gi1alpha.
Mastoparans, a family of tetradecapeptides from wasp venom, have been used as convenient low molecular weight models of receptors coupled to GTP-binding regulatory proteins (G proteins) for the understanding of the interaction between G proteins and receptors. Sukumar and Higashijima have analyzed the conformation of mastoparan-X (MP-X) bound to the G protein alpha-subunit using proton two-dimensional transferred nuclear Overhauser effect (TRNOE) spectroscopy [Sukumar, M., and Higashijima, T. (1992) J. Biol. Chem., 267, 21421-21424]. The resultant structure, however, was not well-defined due to severe overlap of peptide proton resonances. To determine the G protein-bound conformation of MP-X in detail, we have analyzed this interaction by heteronuclear multidimensional TRNOE experiments of MP-X uniformly enriched with 15N and/or 13C. By solving the overlap problem, we were able to determine the precise conformation of MP-X bound to Gi1alpha: the peptide adopts an amphiphilic alpha-helix from Trp3 to C-terminal Leu14, and the atomic root-mean-square deviation (rmsd) values in this portion about the averaged coordinates were 0.27 +/- 0.07 A for the backbone atoms (N, Calpha, C') and 0.84 +/- 0.16 A for all heavy atoms. These values are much smaller than the corresponding rmsd values of the structures obtained from the proton 2D TRNOE spectrum alone: 1.70 +/- 0.41 A for the backbone atoms (N, Calpha, C') and 2.84 +/- 0.51 A for all heavy atoms. Our results indicate that the heteronuclear multidimensional TRNOE experiments of peptides uniformly enriched with stable isotopes are a very powerful tool for analyzing the conformation of short peptides bound to large proteins. We will also discuss the structure-activity relationships of mastoparans in activating G proteins on the basis of the precise structure of MP-X bound to Gi1alpha.
-
==About this Structure==
+
G protein-bound conformation of mastoparan-X: heteronuclear multidimensional transferred nuclear overhauser effect analysis of peptide uniformly enriched with 13C and 15N.,Kusunoki H, Wakamatsu K, Sato K, Miyazawa T, Kohno T Biochemistry. 1998 Apr 7;37(14):4782-90. PMID:9537994<ref>PMID:9537994</ref>
-
1A13 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vespa_simillima_xanthoptera Vespa simillima xanthoptera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A13 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
G protein-bound conformation of mastoparan-X: heteronuclear multidimensional transferred nuclear overhauser effect analysis of peptide uniformly enriched with 13C and 15N., Kusunoki H, Wakamatsu K, Sato K, Miyazawa T, Kohno T, Biochemistry. 1998 Apr 7;37(14):4782-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9537994 9537994]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1a13" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Vespa simillima xanthoptera]]
[[Category: Vespa simillima xanthoptera]]
-
[[Category: Kohno, T.]]
+
[[Category: Kohno T]]
-
[[Category: Kusunoki, H.]]
+
[[Category: Kusunoki H]]
-
[[Category: Miyazawa, T.]]
+
[[Category: Miyazawa T]]
-
[[Category: Sato, K.]]
+
[[Category: Sato K]]
-
[[Category: Wakamatsu, K.]]
+
[[Category: Wakamatsu K]]
-
[[Category: Mast cell degranulation]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:39:01 2008''
+

Current revision

G PROTEIN-BOUND CONFORMATION OF MASTOPARAN-X, NMR, 14 STRUCTURES

PDB ID 1a13

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools