2nzz: Difference between revisions

Revision as of 18:58, 28 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:2nzz.png

Template:STRUCTURE 2nzz

NMR structure analysis of the Penetratin conjugated Gas (374-394) peptideNMR structure analysis of the Penetratin conjugated Gas (374-394) peptide

Template:ABSTRACT PUBMED 17348636

About this StructureAbout this Structure

Full experimental information is available from OCA.

ReferenceReference

Driving forces in the delivery of penetratin conjugated G protein fragment., Albrizio S, Giusti L, D'Errico G, Esposito C, Porchia F, Caliendo G, Novellino E, Mazzoni MR, Rovero P, D'Ursi AM, J Med Chem. 2007 Apr 5;50(7):1458-64. Epub 2007 Mar 10. PMID:17348636

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 {{STRUCTURE_2nzz|  PDB=2nzz  |  SCENE=  }}
-'''NMR structure analysis of the Penetratin conjugated Gas (374-394) peptide'''
+===NMR structure analysis of the Penetratin conjugated Gas (374-394) peptide===
-==Overview==
+<!--
-A42 is a chimera peptide consisting of Galphas(374-394)C379A--the 21-mer C terminus of the Galphas protein, able of adenosine inhibitory activity--and penetratin--the 16 residue fragment, derived from the homeodomain of the Drosophila transcription factor Antennapedia. A42 is able to cross cell membranes and to inhibit A2A and A2B adenosine and beta-adrenergic receptor stimulated camps (D'Ursi et al. Mol. Pharmacol. 2006, 69, 727-36). Here we present an extensive biophysical study of A42 in different membrane mimetics, with the objective to evaluate the molecular mechanisms which promote the membrane permeation. Fluorescence, CD, and NMR data were acquired in the presence of negatively charged and zwitterionic sodium dodecyl sulfate and dodecylphosphocholine surfactants. To validate the spectroscopic results in a larger scale, fluorescence microscopy experiments were performed on negatively charged and zwitterionic dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine vesicles. Our results show that the internalization of A42 is mainly driven by electrostatic interactions, hydrophobic interactions playing only a secondary, sinergistic role. The distribution of the charges along the molecule has an important role, highlighting that internalization is a process which requires a specific matching of peptide and membrane properties.
+The line below this paragraph, {{ABSTRACT_PUBMED_17348636}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17348636 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17348636}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZZ OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NZZ OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Penetratin]]
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