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In-Depth Information
Table 1. Some existing pMHC structure databases freely available for use or download.
Name
Description
URL
PDB
Worldwide repository for the processing and
distribution of 3D structure data of large
molecules of proteins and nucleic acids.
http://www.rcsb.org/pdb/
MPID
A manually curated database on pMHC
interactions containing computed interaction
parameters relevant to each complex.
http://surya.bic.nus.edu.sg/
mpid
MPID-T
A manually curated database containing
computed atomic interaction information on
TCR-pMHC and pMHC complexes obtained
from PDB.
http://surya.bic.nus.edu.sg/
mpidt
FIMM
Database containing HLA 3D experimental
structures obtained from PDB and models
generated by homology modeling.
http://sdmc.lit.org.sg:8080/
fimm/
IMGT/3D
structure-
DB
Database containing annotated information
on the sequences, 2D structures and 3D
structures of TR and pMHC from human and
other vertebrate species according to the
IMGT Scientific chart.
http://imgt3d.igh.cnrs.fr/
3.7 Conclusions
In order to fully understand the phenomenon of pMHC interactions, it is necessary to
introduce structural information. To date, structure-based techniques are poorly
developed and are lagging far behind sequence-based prediction techniques due to
higher complexity in development and computational costs. Despite their slow
progress, structure-based techniques are highly promising as a predictive tool for
vaccine design for its strength in predicting potential T-cell epitopes for MHC
subtypes where insufficient data are available for training sequence-based
procedures.
References
Abagyan, R., and Totrov, M. (1999) Ab initio folding of peptides by the optimal-bias Monte
Carlo minimization procedure. J. Comput. Phys. 151:402-421.
Bernstein, F.C., Koetzle, T.F., Williams, G.J., Meyer, E.E., Brice, M.D., Rodgers, J.R.,
Kennard, O., Shimanouchi, T., and Tasumi, M. (1977) The Protein Data Bank: A com-
puter-based archival file for macromolecular structures. J. Mol. Biol. 112:535-542.
Chothia, C., and Janin, J. (1975) Principles of protein-protein recognition. Nature 28:705-708.
Fernández-Recio, J., Totrov, M., and Abagyan, R. (2002) Soft protein-protein docking in
internal coordinates. Protein Sci. 11:280-291.
Fischer, K.F., and Marquesee, S. (2000) A rapid test for identification of autonomous folding
units in proteins. J. Mol. Biol. 302:701-712.
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