MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2


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MHC-Binding
Epitope  
   
Complex PDB ID 1A1M
Accession Number 3DIEP0376
IEDB ID 65812
Epitope Sequence TPYDINQML
Starting Position1
Ending Position8
Epitope Type Linear Epitope

Assay Information  
Assay Antigen Purified MHC - X-ray crystallography Structure (crystal; NMR; etc.)
PDB CategoryCOMPLEX (ANTIGEN/PEPTIDE)
Keyword MAJOR HISTOCOMPATIBILITY ANTIGEN; MHC; HLA; HLA-B53; HIV; COMPLEX (ANTIGEN/PEPTIDE)
Antibody Residues Interacting with Antigen Open in new window      Download dimplot pdb file
Antibody Chain 1 PDB Chain A
Antigen PDB ChainC
CommentsPositive

Experimental Details
Method
X-RAY DIFFRACTION
Resolution
2.3
R-Value
0.205
Space Group
P 21 21 21
Unit Cell
Length(Å) Angle(°)
a = 50.9 α = 90
b = 82.5 β = 90
c = 109.7 γ = 90



Source Information  
Structure Determination Method X-RAY DIFFRACTION
Host OrganismEscherichia coli
Host Organism StrainBL21 (DE3) PLYSS
Host Taxonomic ID 562
Host Orgism VectorPGMT7
Host Orgism Vector Type PGMT7
PlasmidBL21
  

Ligand non-polymer
 

Sequence


Protein Name
MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2
Poly type
polypeptide(L)
Sequence status
Complete

Primary Sequence

Entity ID
1
Chain ID
A
Source Method
genetically manipulated
Molecule Name
HLA class I histocompatibility antigen, BW-53 B*5301 alpha chain
Sequence Length
278

G S H S M R Y F Y T A M S R P G R G E P R F I A V G Y V D D T Q F V R F D S D A A S P R T E P R P P W I E Q E G P E Y W D R N T Q I F K T N T Q T Y R E N L R I A L R Y Y N Q S E A G S H I I Q R M Y G C D L G P D G R L L R G H D Q S A Y D G K D Y I A L N E D L S S W T A A D T A A Q I T Q R K W E A A R V A E Q L R A Y L E G L C V E W L R R Y L E N G K E T L Q R A D P P K T H V T H H P V S D H E A T L R C W A L G F Y P A E I T L T W Q R D G E D Q T Q D T E L V E T R P A G D R T F Q K W A A V V V P S G E E Q R Y T C H V Q H E G L P K P L T L R W E P H H
The amino acid color is based upon Bob Fletterick's 'Shapely Models'.(Ref. & Table)
Primary Sequence

Entity ID
2
Chain ID
B
Source Method
genetically manipulated
Molecule Name
Beta-2-microglobulin
Sequence Length
99

I Q R T P K I Q V Y S R H P A E N G K S N F L N C Y V S G F H P S D I E V D L L K N G E R I E K V E H S D L S F S K D W S F Y L L Y Y T E F T P T E K D E Y A C R V N H V T L S Q P K I V K W D R D M
The amino acid color is based upon Bob Fletterick's 'Shapely Models'.(Ref. & Table)
Primary Sequence

Entity ID
3
Chain ID
C
Source Method
genetically manipulated
Molecule Name
PEPTIDE TPYDINQML
Sequence Length
9

T P Y D I N Q M L
The amino acid color is based upon Bob Fletterick's 'Shapely Models'.(Ref. & Table)

X-RAY DIFFRACTION

Crystalization

pH
6.5
pH details
18% PEG8000 0.1M SODIUM CACODYLATE PH6.5 0.2M CALCIUM ACETATE


Crystal Data
Unit Cell
Space group
P 21 21 21
Length
Angle
°
a  =
50.9
α  =
90
b  =
82.5
β  =
90
c  =
109.7
γ  =
90


Diffraction
Diffraction Detector
Diffraction radiation
Detector
IMAGE PLATE
Monochromator
Type
SRS BEAMLINE PX9.6
Diffraction Source
Detail
Source
SYNCHROTRON
Collection date
2/9/1996
Type
SRS BEAMLINE PX9.6


Refinement Data
Reflection Details
Structure Solution Method
MOLECULAR REPLACEMENT
Percent Possible(Observed)
97.9
Resolution(High)
2.3
R-Factor(Observed)
0.205
Cut-off Sigma(F)
R-Work
0.205
Number Reflections(Observed)
88881
R-Free
No. of Non-Hydrogen atoms
Used in Refinement
Protein atom
3184
Nucleic acid atom
Heterogen Atoms
Solvent Atoms
187
Total Atoms
3371


Software and Computing
Computing
Software
Data Reduction (intensity integration)
DENZO
model building
Data Reduction (data scaling)
SCALEPACK
refinement
X-PLOR 3.1
Structure Solution
X-PLOR 3.1
Structure Refinement
X-PLOR 3.1

GO functional annotation for 1a1m



Literature reference

Title
Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.
Authors
Journal
Year
Journal Volume
First Page
Last Page
PubMed Abstract
The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles; the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove; bound water molecules; acting in concert with the side chains of polymorphic residues; provide the functional malleability of the MHC; which enables the high affinity/low specificity binding of multiple peptide epitopes.
PubMed ID
Search related article in PubMed
Keywords
MAJOR HISTOCOMPATIBILITY ANTIGEN; MHC; HLA; HLA-B53; HIV; COMPLEX (ANTIGEN/PEPTIDE)




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Ag-Ab Interaction of the1A1M between chain "C" and chain "A"



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Epitope found in chain   :C                                                                                           
Epitope Sequence:-TPYDINQML
Epitope Position found in PDB File   :   1-8  (Highlighted in white spacefill model)
T P Y D I N Q M L

Download PDB File Download Ag-Ab Interaction PDB File

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Reference :
Herraez, Angel (2006), "Biomolecules in the Computer: Jmol to the Rescue", Biochemistry and Molecular Biology Education 34 (4): 255-261.



Links to external databases and resources



The IEDB contains data related to antibody and T cell epitopes for humans, non-human primates, rodents, and other animal species. Curation of peptidic epitope data relating to all infectious diseases.
Bcipep is collection of the peptides having the role in Humoral immunity. The peptides in the database has varying measure of immunogenicity.This database can assist in the development of method for predicting B cell epitopes, desigining synthetic vaccines and in disease diagnosis.
A DATABASE OF MHC LIGANDS AND PEPTIDE MOTIFS (Ver. 1.0) SYFPEITHI is a database comprising more than 7000 peptide sequences known to bind class I and class II MHC molecules. The entries are compiled from published reports only.
The HIV databases contain data on HIV genetic sequences, immunological epitopes, drug resistance-associated mutations, and vaccine trials. The website also gives access to a large number of tools that can be used to analyze these data. This project is funded by the Division of AIDS of the National Institute of Allergy and Infectious Diseases (NIAID), a part of the National Institutes of Health (NIH). Click on any of the links below to access a database.
The aim of ABCpred server is to predict B cell epitope(s) in an antigen sequence, using artificial neural network. This is the first server developed based on recurrent neural network (machine based technique) using fixed length patterns.
EPIPREDICT is a new and reliable software to predict HLA-class II restricted T cell epitopes and ligands.
Expasy ProtScale ProtScale [Reference / Documentation] allows you to compute and represent the profile produced by any amino acid scale on a selected protein.
MHCBN is a curated database consisting of detailed information about major histocompatibility complex (MHC) binding, non-binding peptides, and T-cell epitopes. Version 4.0 provides information about peptides interacting with TAP and MHC-linked autoimmune diseases.
AntiJen v2.0 is a database containing quantitative binding data for peptides binding to MHC ligands, TCR-MHC complexes, T cell epitopes, TAP, B cell epitope molecules, and immunological protein-protein interactions. AntiJen includes a peptide library, copy numbers, and diffusion coefficient data. All entries are from published experimentally determined data. The database currently holds over 24,000 entries. No data in AntiJen is from prediction experiments.
HLA Peptide Binding Predictions Function: Rank potential 8-mer, 9-mer, or 10-mer peptides based on a predicted half-time of dissociation to HLA class I molecules. The analysis is based on coefficient tables deduced from the published literature by Dr. Kenneth Parker, Children's Hospital Boston (email: kenneth.parker@childrens.harvard.edu ). Another web site for predicting which peptides bind to MHC molecules is SYFPEITHI, developed by Hans-Georg Rammensee's lab.
AllergenOnline provides access to a peer reviewed allergen list and sequence searchable database intended for identifying proteins that may present a potential risk of allergenic cross-reactivity. This website was designed to help in assessing the safety of proteins that may be introduced into foods through genetic engineering or food processing methods.
The I.U.I.S. Allergen Nomenclature Sub-committee operates under the auspices of the International Union of Immunological Societies (I.U.I.S.) and the World Health Organisation (W.H.O.). The objectives of the I.U.I.S. Allergen Nomenclature Sub-committee are to Maintain a unique and unambiguous nomenclature for allergen molecules and Maintain the ‘official list of allergens’.
Superficial is tool for the identification of potential epitopes or binding sites.
UMAS is a server which provides mirrors of a list of various epitope prediction tools and databases.
MAPPP will predict possible antigenic peptides to be processed and finally presented on cell surfaces. This database aides in the prediction of immunodominant T-cell epitopes and is able to predict the proteasomal cleavage of proteins into smaller fragments, and the binding of peptide sequences to MHC class I molecules.
JenPepM is a database of quantitative binding data for immunological protein-peptide interactions, which allows speedy access to binding data through simple on-line interfaces and effective search mechanisms.
Protall database contains biochemical and clinical information about plant food allergens involved in classical IgE-induced hypersensitivity reactions about 77 allergens from 48 plant species. There are many foods for which a case history of an allergic reaction has been reported for which the allergens responsible have not been described. These are not included in the database.
IMGT®, the international ImMunoGeneTics information system is a high-quality integrated knowledge resource specialized in the immunoglobulins (IG), T cell receptors (TR), major histocompatibility complex (MHC), immunoglobulin superfamily (IgSF), major histocompatibility complex superfamily (MhcSF) and related proteins of the immune system (RPI) of human and other vertebrate species.