From Proteopedia
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| - | [[Image:1jav.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1jav| PDB=1jav | SCENE= }} | | {{STRUCTURE_1jav| PDB=1jav | SCENE= }} |
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| - | '''AVERAGE NMR SOLUTION STRUCTURE OF THE TRP-RICH PEPTIDE OF HIV GP41 BOUND TO DPC MICELLES'''
| + | ===AVERAGE NMR SOLUTION STRUCTURE OF THE TRP-RICH PEPTIDE OF HIV GP41 BOUND TO DPC MICELLES=== |
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| - | ==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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11583156}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11583156 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11583156}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1JAV is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAV OCA]. | + | 1JAV is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAV OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Vogel, H J.]] | | [[Category: Vogel, H J.]] |
| | [[Category: Amphipathic alpha helix]] | | [[Category: Amphipathic alpha helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:59:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 19:11:09 2008'' |
Revision as of 16:16, 1 July 2008
Template:STRUCTURE 1jav
AVERAGE NMR SOLUTION STRUCTURE OF THE TRP-RICH PEPTIDE OF HIV GP41 BOUND TO DPC MICELLES
Template:ABSTRACT PUBMED 11583156
About this Structure
1JAV 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
Page seeded by OCA on Tue Jul 1 19:11:09 2008
