1zec: Difference between revisions

Revision as of 04:09, 29 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:1zec.png

Template:STRUCTURE 1zec

NMR SOLUTION STRUCTURE OF NEF1-25, 20 STRUCTURESNMR SOLUTION STRUCTURE OF NEF1-25, 20 STRUCTURES

Template:ABSTRACT PUBMED 9166767

About this StructureAbout this Structure

1ZEC is a Single protein structure of sequence from Human immunodeficiency virus 1. Full experimental information is available from OCA.

ReferenceReference

Solution structure of a polypeptide from the N terminus of the HIV protein Nef., Barnham KJ, Monks SA, Hinds MG, Azad AA, Norton RS, Biochemistry. 1997 May 20;36(20):5970-80. PMID:9166767

Page seeded by OCA on Tue Jul 29 04:09:26 2008

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-[[Image:1zec.gif|left|200px]]
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 {{STRUCTURE_1zec|  PDB=1zec  |  SCENE=  }}
-'''NMR SOLUTION STRUCTURE OF NEF1-25, 20 STRUCTURES'''
+===NMR SOLUTION STRUCTURE OF NEF1-25, 20 STRUCTURES===
-==Overview==
+<!--
-Nef is a 27 kDa myristylated phosphoprotein expressed early in infection by HIV. The N terminus of Nef is thought to play a vital role in the functions of this protein through its interactions with membrane structures. The solution structure of a 25-residue polypeptide corresponding to the N terminus of Nef (Nef1-25) has been investigated by 1H NMR spectroscopy. In aqueous solution at pH 4.8 and 281 K, this peptide underwent conformational averaging, with Pro13 existing in cis and trans conformations in nearly equal proportions. In methanol solution, however, the peptide adopted a well-defined alpha-helical structure from residues 6 to 22, with the N- and C-terminal regions having a less ordered structure. On the basis of a comparison of chemical shifts and NOEs, it appeared that this helical structure was maintained in aqueous trifluoroethanol (50% v/v) and to a lesser extent in a solution of SDS micelles. When the N-acetyl group was replaced by either an N-myristyl or a free ammonium group, there was little effect on the three-dimensional structure of the peptide in methanol; deamidation of the C terminus also had no effect on the structure in methanol. In water, the myristylated peptide aggregated. The similarity between the sequences of Nef1-25 and melittin is reflected in the similar structures of the two molecules, although the N-terminal helix of melittin is more defined. This similarity in structure raises the possibility that Nef1-25 not only interacts with membranes but also may be capable of disrupting them and causing cell lysis. This type of interaction could contribute at least in part to the killing of bystander cells in lymphoid tissues during HIV infection.
+The line below this paragraph, {{ABSTRACT_PUBMED_9166767}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9166767 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9166767}}
 ==About this Structure==
-ZEC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZEC OCA].
+ZEC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZEC OCA].
 ==Reference==
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 [[Category: Polypeptide]]
 [[Category: Viral peptide]]
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