DIMACS TR: 2002-18
The set of pair-wise correlated sequence positions contributes to determination of the immunoglobulin fold
Authors: Boris Galitsky, Andrey Dementiev and Sergey Shelepin
ABSTRACT
In this study, we are resolving the contradiction that rather limited
number of residues or classes of amino acids (about 10) determines the
fold (Immunoglobulin-like) for the sequence of about 100 residues long.
Immunoglobulin fold comprises the protein super-families with rather
distinguishing sequences with less than 10% identity; their sequence
alignment can be accomplished only taking into account the 3D structure.
Therefore, we believe that discovering the additional common features of
the sequences is necessary to explain the existence of common fold for
these (SCOP) superfamilies. The analysis of pair-wise interconnection
between residues of the multiple sequence alignment helped us to reveal
the set of mutually correlated positions, inherent to almost every
super-family of protein fold. Hence, the set of constant positions plus
the set of variable but mutually correlated ones can serve as a basis of
having the common 3D structure for rather distinguishing protein
sequences.
Paper Available at:
ftp://dimacs.rutgers.edu/pub/dimacs/TechnicalReports/TechReports/2002/2002-18.ps.gz
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