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- PDB-1p5a: Conformational Mapping of the N-terminal Peptide of HIV-1 GP41 in... -
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Basic information
Entry | Database: PDB / ID: 1p5a | ||||||
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Title | Conformational Mapping of the N-terminal Peptide of HIV-1 GP41 in lipid detergent and aqueous environments using 13C-enhanced Fourier Transform Infrared Spectroscopy | ||||||
![]() | Envelope polyprotein GP160 | ||||||
![]() | VIRAL PROTEIN / human immunodeficiency virus (HIV-1) / viral fusion peptide / gp41 | ||||||
Function / homology | ![]() Dectin-2 family / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane ...Dectin-2 family / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / membrane Similarity search - Function | ||||||
Method | INFRARED SPECTROSCOPY / molecular dynamics | ||||||
![]() | Gordon, L.M. / Mobley, P.W. / Lee, W. / Eskandari, S. / Kaznessis, Y.N. / Sherman, M.A. / Waring, A.J. | ||||||
![]() | ![]() Title: Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy. Authors: Gordon, L.M. / Mobley, P.W. / Lee, W. / Eskandari, S. / Kaznessis, Y.N. / Sherman, M.A. / Waring, A.J. #1: ![]() Title: CONFORMATIONAL MAPPING OF THE N-TERMINAL PEPTIDE OF HIV-1 GP41 IN MEMBRANE ENVIRONMENTS USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY Authors: GORDON, L.M. / MOBLEY, P.W. / PILPA, R. / SHERMAN, M.A. / WARING, A.J. | ||||||
History |
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Remark 250 | REMARK: THIS STRUCTURE WAS DETERMINED BY MEANS OF 13C-ENHANCED FOURIER TRANSFORM INFRARED ...REMARK: THIS STRUCTURE WAS DETERMINED BY MEANS OF 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR). DATA SET CONSISTS OF 19 CONFORMERS DERIVED FROM MOLECULAR DYNAMICS IN A MODELED SDS MICELLE SURROUNDED BY WATER WITH PEPTIDE BACKBONE CONSTRAINTS FROM FTIR. EXPERIMENTAL DETAILS EXPERIMENT TYPE : INFRARED SPECTROSCOPY TEMPERATURE (KELVIN) : 298 PH : 7.4 IONIC STRENGTH : 0.271 PRESSURE : AMBIENT SAMPLE CONTENTS : THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES 519,521,523,524,525,526,527, 528,529,530,531,532,533,534,538,539. EXPERIMENTS CONDUCTED : 13C-ISOTOPE ENHANCED FTIR SPECTROMETER FIELD STRENGTH : NULL SPECTROMETER MODEL : RESEARCH SERIES SPECTROMETER MANUFACTURER : MATTSON FTIR STRUCTURE DETERMINATION. SOFTWARE USED : WINFIRST FTIR CURVE FITTING SOFTWARE METHOD USED : MOLECULAR DYNAMICS CONFORMERS, NUMBER CALCULATED : 20 CONFORMERS, NUMBER SUBMITTED : 19 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE COVALENT GEOMETRY BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK: THE COORDINATES IN THIS ENTRY WERE GENERATED FROM 13-C INDUCED SPECTRAL SHIFTS WHICH GIVE RESIDUE-SPECIFIC SECONDARY STRUCTURE INFORMATION. PEPTIDE CONCENTRATION WAS 47 MICROMOLAR. PEPTIDE/SDS RATIO WAS 1/200. FTIR SPECTRA WERE AVERAGED OVER 256 SCANS AT A GAIN OF 4 AND A RESOLUTION OF 2 CM-1 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 105.8 KB | Display | ![]() |
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PDB format | ![]() | 82.6 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 424.1 KB | Display | ![]() |
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Full document | ![]() | 434.4 KB | Display | |
Data in XML | ![]() | 8.4 KB | Display | |
Data in CIF | ![]() | 14.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2123.481 Da / Num. of mol.: 1 / Fragment: residues 519-541 / Source method: obtained synthetically Details: The sequence of this peptide occurs naturally in human immunodeficiency virus glycoprotein 41. References: UniProt: P03377 |
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-Experimental details
-Experiment
Experiment | Method: INFRARED SPECTROSCOPY |
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NMR experiment | Type: 13C-isotope enhanced FTIR |
NMR details | Text: The coordinates in this entry were generated from 13-C induced spectral shifts which give residue-specific secondary structure information. Peptide concentration was 47 micromolar. Peptide/SDS ...Text: The coordinates in this entry were generated from 13-C induced spectral shifts which give residue-specific secondary structure information. Peptide concentration was 47 micromolar. Peptide/SDS ratio was 1/200. FTIR spectra were averaged over 256 scans at a gain of 4 and a resolution of 2 cm-1 |
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Sample preparation
Details | Contents: THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES ...Contents: THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES 519,521,523,524,525,526,527,528,529,530,531,532,533,534,538,539. Solvent system: 94 mM SDS (sodium dodecyl sulfate) in deuterated PBS (phosphate buffered saline), where PBS is 120 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4 |
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Sample conditions | Ionic strength: 0.271 / pH: 7.4 / Pressure: ambient / Temperature: 298 |
Crystal grow | *PLUS Method: spectroscopy / Details: spectroscopy |
-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Mattson FTIR Research Series / Manufacturer: Mattson FTIR / Model: Research Series |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 Details: The system of more than 16,000 atoms (peptide, SDS micelle, water, sodium counterions) was simulated for 2.5 nanoseconds at a constant pressure P=1 atm and constant temperature T=303.15 K. | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 20 / Conformers submitted total number: 19 |