1jau: Difference between revisions

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[[Image:1jau.gif|left|200px]]
{{Seed}}
[[Image:1jau.png|left|200px]]


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{{STRUCTURE_1jau|  PDB=1jau  |  SCENE=  }}  
{{STRUCTURE_1jau|  PDB=1jau  |  SCENE=  }}  


'''NMR Solution Structure of the Trp-Rich Peptide of HIV gp41 Bound to DPC Micelles'''
===NMR Solution Structure of the Trp-Rich Peptide of HIV gp41 Bound to DPC Micelles===




==Overview==
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The membrane-proximal tryptophan-rich region of the HIV transmembrane glycoprotein, gp41, plays an important role in the membrane fusion reaction. Using NMR spectroscopy, we have studied the tertiary structure of a synthetic 19-residue amidated peptide (NH2-KWASLWNWFNITNWLWYIK-CONH2) corresponding to this region in membrane-mimetic environments. Initial experiments in sodium dodecyl sulfate/H2O micelles and trifluoroethanol gave poor results, because of low solubility. However, in dodecylphosphocholine micelles, we obtained excellent 500 and 800 MHz NMR spectra, suggesting that the peptide has a preference for a zwitterionic membrane-like environment. The final NMR structures demonstrated a well-defined helical peptide with a backbone rmsd of 0.47 +/- 0.18 A. Four of the five tryptophan residues, as well as the tyrosine residue, formed a "collar" of aromatic residues along the axial length of the helix. By analogy to related tryptophan-rich antimicrobial peptides, the structure indicates that the aromatic residues of the HIV peptide are positioned within the membrane-water interface of a phospholipid bilayer. This is confirmed by the observation of direct NOEs between the aromatic residues of the peptide to the headgroup and interfacial protons of prototonated dodecylphosphocholine. The bulk of the polar residues are positioned on one face of this structure, with the hydrophobic phenylalanine side chain on the opposing face, forming an amphipathic structure. This work shows that the Trp-rich membrane-proximal region of HIV and related viruses can bind to the surfaces of zwitterioninc membranes in a "Velcro-like" manner.
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{{ABSTRACT_PUBMED_11583156}}


==About this Structure==
==About this Structure==
1JAU is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAU OCA].  
1JAU is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAU OCA].  


==Reference==
==Reference==
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[[Category: Vogel, H J.]]
[[Category: Vogel, H J.]]
[[Category: Amphipathic alpha helix]]
[[Category: Amphipathic alpha helix]]
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Revision as of 23:07, 28 July 2008

File:1jau.png

Template:STRUCTURE 1jau

NMR Solution Structure of the Trp-Rich Peptide of HIV gp41 Bound to DPC Micelles

Template:ABSTRACT PUBMED 11583156

About this Structure

1JAU is a Single protein structure. Full experimental information is available from OCA.

Reference

The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles., Schibli DJ, Montelaro RC, Vogel HJ, Biochemistry. 2001 Aug 14;40(32):9570-8. PMID:11583156

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