Alpha This is a work in progress and may change. Your feedback is very welcome.
  


7EMC

SLA-1*01:01 binding "ATEIRELLV" at 1.90Å resolution

Data provenance

Structure downloaded from PDB Europe using the Coordinate Server. Aligned to residues 1-180 of 1HHK2 using the CEALIGN3 function of PyMol4. Chain assigment using a Levenshtein distance5 method using data from the PDBe REST API6. Organism data from PDBe REST API. Data for both of these operations from the Molecules endpoint. Structure visualised with 3DMol7.

Information sections


Complex type

Class i with peptide

1. Beta 2 microglobulin
['B', 'E', 'H']
2. Class I alpha
SLA-1*01:01
['A', 'D', 'G']
3. Peptide
ATEIRELLV
['C', 'F', 'I']

Species


Locus / Allele group


Publication

Mooring Stone-Like Arg114 Pulls Diverse Bulged Peptides: First Insight into African Swine Fever Virus-Derived T Cell Epitopes Presented by Swine Major Histocompatibility Complex Class I.

Yue C, Xiang W, Huang X, Sun Y, Xiao J, Liu K, Sun Z, Qiao P, Li H, Gan J, Ba L, Chai Y, Qi J, Liu P, Qi P, Zhao Y, Li Y, Qiu HJ, Gao GF, Gao G, Liu WJ
J Virol (2022) 96, e0137821 [doi:10.1128/JVI.01378-21]  [pubmed:34851145

Abstract Serum samples of 20 hospitalized COVID-19 patients from Brazil who were infected by the earlier SARS-CoV-2 lineages B.1.1.28 and B.1.1.33, and by the variant of concern (VOC) Gamma (P.1) were tested by plaque reduction neutralization test (PRNT90) with wild isolates of a panel of SARS-CoV-2 lineages, including B.1, Zeta, N.10, and the VOCs Gamma, Alpha, and Delta that emerged in different timeframes of the pandemic. The main objective of the present study was to evaluate if serum of patients infected by earlier lineages was capable to neutralize later emerged VOCs. We also evaluated if the four-fold difference in PRNT90 titers is a reliable seropositivity criterion to distinguish infections caused by different SARS-CoV-2 lineages. Sera collected between May 2020 and August 2021 from the day of admittance to the hospital to 21 days after diagnostic of patients infected by the two earlier lineages B.1.1.28 and B.1.1.33 presented neutralizing capacity for all challenged VOCs, including Gamma and Delta. Among all variants tested, Delta and N.10 presented the lowest geometric mean of neutralizing antibody titers, and B.1.1.7, presented the highest titers. Four patients infected with Gamma, that emerged in December 2020, presented neutralizing antibodies for B.1, B.1.1.33 and B.1.1.28, its ancestor lineage. All of them had neutralizing antibodies under the level of detection for the VOC Delta. Patients infected by B.1.1.28 presented very similar geometric mean of neutralizing antibody titers for both B.1.1.33 and B.1.1.28. Findings presented here indicate that most patients infected in early stages of COVID-19 pandemic presented neutralizing antibodies capable to neutralize wild types of all later emerged VOCs in Brazil, and that the four-fold difference in PRNT90 titers is not reliable to distinguish humoral response among different SARS-CoV-2 lineages.

Structure deposition and release

Deposited: 2021-04-13
Released: 2021-12-08
Revised: 2022-03-16

Data provenance

Publication data retrieved from PDBe REST API8 and PMCe REST API9

Other structures from this publication


Peptide details

Length: Nonamer (9 amino acids)

Sequence: ATEIRELLV

Interactive view
Cutaway side view (static)
Surface top view (static - coloured by atom property)
Cutaway top view (static)

Data provenance

MHC:peptide complexes are visualised using PyMol. The peptide is superimposed on a consistent cutaway slice of the MHC binding cleft (displayed as a grey mesh) which best indicates the binding pockets for the P1/P5/PC positions (side view - pockets A, E, F) and for the P2/P3/PC-2 positions (top view - pockets B, C, D). In some cases peptides will use a different pocket for a specific peptide position (atypical anchoring). On some structures the peptide may appear to sterically clash with a pocket. This is an artefact of picking a standardised slice of the cleft and overlaying the peptide.


Peptide neighbours

P1 ALA

TYR171
LYS66
LEU5
LEU163
SER167
TYR159
TYR59
TYR7
GLU63
P2 THR

TYR159
TYR7
TYR99
TYR9
GLU63
MET45
LEU163
LYS66
GLN67
P3 GLU

LYS66
ARG114
TYR159
GLN67
TYR9
ARG156
THR70
TYR99
ARG155
P4 ILE

THR70
LYS66
P5 ARG

ARG156
THR70
P6 GLU

THR70
TYR9
TYR74
TYR116
TYR95
ARG114
THR73
ARG156
TRP147
SER97
P7 LEU

ALA150
LYS146
VAL152
THR73
ARG156
TRP147
P8 LEU

GLY77
LYS146
ASN80
THR73
VAL76
TRP147
P9 VAL

LEU81
TRP147
GLY77
LYS146
ASN80
TYR84
TYR123
TYR95
THR143

Colour key

Aromatic Hydrophobic Acidic Basic Neutral/polar

Data provenance

Neighbours are calculated by finding residues with atoms within 5Å of each other using BioPython Neighboursearch module. The list of neighbours is then sorted and filtered to inlcude only neighbours where between the peptide and the MHC Class I alpha chain.

Colours selected to match the YRB scheme. [https://www.frontiersin.org/articles/10.3389/fmolb.2015.00056/full]


Binding cleft pockets


Peptide sidechain binding pockets (static)
Peptide terminii and backbone binding residues (static)
A Pocket

TYR159
LEU163
SER167
TYR171
LEU5
TYR59
GLU63
LYS66
TYR7
B Pocket

ALA24
VAL34
MET45
GLU63
LYS66
GLN67
TYR7
THR70
TYR9
TYR99
C Pocket

THR70
THR73
TYR74
TYR9
SER97
D Pocket

ARG114
ARG155
ARG156
TYR159
LEU160
TYR99
E Pocket

ARG114
TRP147
VAL152
ARG156
SER97
F Pocket

TYR116
TYR123
THR143
LYS146
TRP147
GLY77
ASN80
LEU81
TYR84
TYR95

Colour key

Binds N-terminus Binds P1 backbone Binds P2 backbone Binds PC-1 backbone Binds C-terminus

Data provenance

N-/C-terminus and peptide backbone binding residues are assigned according to previously published information and pockets are assigned according to an adaptation of a previously published set of residues. All numbering is currently that of the 'canonical' structures of human and mouse MHC Class I molecules.

Chain sequences

1. Beta 2 microglobulin
Beta 2 microglobulin
        10        20        30        40        50        60
EFVARPPKVQVYSRHPAENGKPNYLNCYVSGFHPPQIEIDLLKNGEKMNAEQSDLSFSKD
        70        80        90
WSFYLLVHTEFTPNAVDQYSCRVKHVTLDKPKIVKWDRDH

2. Class I alpha
SLA-1*01:01
        10        20        30        40        50        60
GPHSLSYFYTAVSRPDRGDSRFIAVGYVDDTQFVRFDSDAPNPRMEPRAPWIQQEGQDYW
        70        80        90       100       110       120
DRETRKQRDTSQTYRVGLKNLRGYYNQSEAGSHTYQSMYGCYLGPDGLLLRGYRQYAYDG
       130       140       150       160       170       180
ADYIALNEDLRSWTAADTAAQITKRKWETANVAERRRSYLQGLCVESLREYLEMGKDTLQ
       190       200       210       220       230       240
RAEPPKTHVTRHPSSDLGVTLRCWALGFYPKEISLTWQREGQDQSQDMELVETRPSGDGT
       250       260       270
FQKWAALVVPPGEEQSYTCHVQHEGLQEPLTLRWD

3. Peptide
ATEIRELLV


Data provenance

Sequences are retrieved via the Uniprot method of the RSCB REST API. Sequences are then compared to those derived from the PDB file and matched against sequences retrieved from the IPD-IMGT/HLA database for human sequences, or the IPD-MHC database for other species. Mouse sequences are matched against FASTA files from Uniprot. Sequences for the mature extracellular protein (signal petide and cytoplasmic tail removed) are compared to identical length sequences from the datasources mentioned before using either exact matching or Levenshtein distance based matching.


Downloadable data

Data can be downloaded to your local machine from the links below.
Clicking on the clipboard icon will copy the url for the data to your clipboard.
This can then be used to load the structure/data directly from the url into an application like PyMol (for 3D structures) using the load command:
   e.g. load http://www.histo.fyi/structures/downloads/1hhk_1_peptide.cif
or in the case of JSON formatted files to retrieve it and use it as part of notebooks such as Jupyter or GoogleColab.
Please take note of the data license. Using data from this site assumes that you have read and will comply with the license.

Complete structures

Aligned structures [cif]
  1. 7EMC assembly 1  
  2. 7EMC assembly 2  
  3. 7EMC assembly 3  

Components

MHC Class I alpha chain [cif]
  1. 7EMC assembly 1  
  2. 7EMC assembly 2  
  3. 7EMC assembly 3  
MHC Class I antigen binding domain (alpha1/alpha2) [cif]
  1. 7EMC assembly 1  
  2. 7EMC assembly 2  
  3. 7EMC assembly 3  
Peptide only [cif]
  1. 7EMC assembly 1  
  2. 7EMC assembly 2  
  3. 7EMC assembly 3  

Derived data

Data for this page [json]
https://api.histo.fyi/v1/structures/7emc

Data license

The data above is made available under a Creative Commons CC-BY 4.0 license. This means you can copy, remix, transform, build upon and redistribute the material, but you must give appropriate credit, provide a link to the license, and indicate if changes were made.
If you use any data downloaded from this site in a publication, please cite 'https://www.histo.fyi/'. A preprint is in preparation.

Footnotes