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- PDB-1erf: CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1erf | ||||||
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Title | CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 GP41 USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR) | ||||||
![]() | TRANSMEMBRANE GLYCOPROTEIN | ||||||
![]() | 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 / apoptotic process / host cell plasma membrane / structural molecule activity / virion membrane / membrane Similarity search - Function | ||||||
Method | INFRARED SPECTROSCOPY / molecular dynamics, simulated annealing | ||||||
![]() | Gordon, L.M. / Mobley, P.W. / Pilpa, R. / Sherman, M.A. / Waring, A.J. | ||||||
![]() | ![]() Title: Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using (13)C-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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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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-Validation report
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-Related structure data
Similar structure data |
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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: N-TERMINAL FUSION PEPTIDE (RESIDUES 519-541) / Mutation: C-TERMINUS HAS BEEN AMIDATED / 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: 13-C 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. |
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Sample preparation
Crystal | Description: This structure was determined by means of 13C-enhanced Fourier Transform Infrared Spectroscopy (FTIR). Data set consists of 17 conformers derived from simulated annealing with constraints from FTIR. |
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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: 70% hexafluoroisopropanol (HFIP), 29.9% water, 0.1% formic acid (v/v) |
Sample conditions | Ionic strength: 0 / pH: 7 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: infrared spectroscopy |
-Data collection
NMR spectrometer | Type: Mattson FTIR Research Series / Manufacturer: Mattson FTIR / Model: Research Series / Field strength: 0 MHz |
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Processing
NMR software |
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Refinement | Method: molecular dynamics, simulated annealing / Software ordinal: 1 Details: Molecular dynamics (simulated annealing) was used to generate an ensemble of conformers consistent with the FTIR data. | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 31 / Conformers submitted total number: 17 |