CRYSTAL STRUCTURE OF HLA-A*0201 COMPLEXED WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL GROUP SUBSTITUTED BY A METHYL GROUP


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MHC-Binding
Epitope  
   
Complex PDB ID 1B0R
Accession Number 3DIEP0337
IEDB ID 20351
Epitope Sequence GILGFVFTL
Starting Position701
Ending Position706
Epitope Type Linear Epitope

Assay Information  
Assay Antigen Purified MHC - X-ray crystallography Structure (crystal; NMR; etc.)
PDB CategorySIGNALING PROTEIN
Keyword HLA-A2; ANTIGENIC PEPTIDES; CLASS I MHC MOLECULES; HLA-A2 COMPLEXES; HYDROGEN BONDS; PROTEIN STRUCTURE; SIGNALING PROTEIN
Antibody Residues Interacting with Antigen Open in new window      Download dimplot pdb file
Antibody Chain 1 PDB Chain A
Antigen PDB ChainC
CommentsNo interpretable electron density was observed at the P4-Gly and P5-Phe positions of the peptide.

Experimental Details
Method
X-RAY DIFFRACTION
Resolution
2.9
R-Value
0.253
Space Group
P 21 21 21
Unit Cell
Length(Å) Angle(°)
a = 49.6 α = 90
b = 74.4 β = 90
c = 121.4 γ = 90



Source Information  
Structure Determination Method X-RAY DIFFRACTION
Host OrganismEscherichia coli
Host Organism StrainXA90
Host Taxonomic ID 562
PlasmidPHN1
  

Ligand L-peptide linking
 

Sequence


Protein Name
CRYSTAL STRUCTURE OF HLA-A*0201 COMPLEXED WITH A PEPTIDE WITH THE CARBOXYL-TERMINAL GROUP SUBSTITUTED BY A METHYL GROUP
Poly type
polypeptide(L)
Sequence status
Complete

Primary Sequence

Entity ID
1
Chain ID
A
Source Method
genetically manipulated
Molecule Name
PROTEIN (HLA-A*0201)
Fragment Name
EXTRACELLULAR DOMAINS ALPHA 1,ALPHA 2 AND ALPHA 3
Sequence Length
275

G S H S M R Y F F T S V 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 Q R M E P R A P W I E Q E G P E Y W D G E T R K V K A H S Q T H R V D L G T L R G Y Y N Q S E A G S H T V Q R M Y G C D V G S D W R F L R G Y H Q Y A Y D G K D Y I A L K E D L R S W T A A D M A A Q T T K H K W E A A H V A E Q L R A Y L E G T C V E W L R R Y L E N G K E T L Q R T D A P K T H M T H H A V S D H E A T L R C W A L S 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 G T F Q K W A A V V V P S G Q E Q R Y T C H V Q H E G L P K P L T L R W E
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
PROTEIN (HLA-A*0201)
Fragment Name
BETA 2 MICROGLOBULIN
Sequence Length
100

M 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
Synthetic
Molecule Name
PROTEIN (INFLUENZA MATRIX PEPTIDE)
Sequence Length
9

G I L G F V F T C D E
The amino acid color is based upon Bob Fletterick's 'Shapely Models'.(Ref. & Table)

X-RAY DIFFRACTION

Crystalization

pH
6.5
pH details
pH 6.50


Crystal Data
Unit Cell
Space group
P 21 21 21
Length
Angle
°
a  =
49.6
α  =
90
b  =
74.4
β  =
90
c  =
121.4
γ  =
90


Diffraction
Diffraction Detector
Diffraction radiation
Detector
IMAGE PLATE
Monochromator
Type
Diffraction Source
Detail
Source
Collection date
Type


Refinement Data
Reflection Details
Structure Solution Method
MOLECULAR REPLACEMENT
Percent Possible(Observed)
90.5
Resolution(High)
2.9
R-Factor(Observed)
0.253
Cut-off Sigma(F)
2
R-Work
0.253
Number Reflections(Observed)
8304
R-Free
No. of Non-Hydrogen atoms
Used in Refinement
Protein atom
3092
Nucleic acid atom
0
Heterogen Atoms
0
Solvent Atoms
0
Total Atoms
3092


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
Structure Refinement
X-PLOR 3.1

GO functional annotation for 1b0r



Literature reference

Title
Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino- or carboxyl-terminal group substituted by a methyl group.
Authors
Journal
Year
Journal Volume
First Page
Last Page
PubMed Abstract
The crystal structures of class I major histocompatibility complex (MHC) molecules complexed with antigenic peptides revealed a network of hydrogen bonds between the charged amino- and carboxyl-termini of the peptides and conserved MHC residues at both ends of the peptide binding site. These interactions were shown to contribute substantially to the stability of class I MHC/peptide complexes by thermal denaturation studies using synthetic peptides in which either the amino- or carboxyl-terminal group is substituted by a methyl group. Here we report crystal structures of HLA-A*0201 complexed with these terminally modified synthetic peptides showing that they adopt the same bound conformation as antigenic peptides. A number of variations in peptide conformation were observed for the terminally modified peptides; including in one case; a large conformational difference in four central peptide residues that is apparently caused by the lattice contact. This is reminiscent of the way binding a T-cell receptor changed the conformation of central residues of an MHC-bound peptide. The structures determined identify which conserved hydrogen bonds are eliminated in terminally substituted peptides and suggest an increased energetic importance of the interactions at the peptide termini for MHC-peptide stability.
PubMed ID
Search related article in PubMed
Keywords
HLA-A2; ANTIGENIC PEPTIDES; CLASS I MHC MOLECULES; HLA-A2 COMPLEXES; HYDROGEN BONDS; PROTEIN STRUCTURE; SIGNALING PROTEIN




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Ag-Ab Interaction of the1B0R between chain "C" and chain "A"



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Epitope found in chain   :C                                                                                           
Epitope Sequence:-GILGFVFTL
Epitope Position found in PDB File   :   701-706  (Highlighted in white spacefill model)
G I L G F V F T C D E

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.