MALISAM: A database of structurally analogous motifs in proteins

Hua Cheng, Bong Hyun Kim, Nick V. Grishin

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

Abstract

MALISAM (manual alignments for structurally analogous motifs) represents the first database containing pairs of structural analogs and their alignments. To find reliable analogs, we developed an approach based on three ideas. First, an insertion together with a part of the evolutionary core of one domain family (a hybrid motif) is analogous to a similar motif contained within the core of another domain family. Second, a motif at an interface, formed by secondary structural elements (SSEs) contributed by two or more domains or subunits contacting along that interface, is analogous to a similar motif present in the core of a single domain. Third, an artificial protein obtained through selection from random peptides or in sequence design experiments not biased by sequences of a particular homologous family, is analogous to a structurally similar natural protein. Each analogous pair is superimposed and aligned manually, as well as by several commonly used programs. Applications of this database may range from protein evolution studies, e.g. development of remote homology inference tools and discriminators between homologs and analogs, to protein-folding research, since in the absence of evolutionary reasons, similarity between proteins is caused by structural and folding constraints. The database is publicly available at http://prodata.swmed.edu/malisam.

Original languageEnglish (US)
Pages (from-to)D211-D217
JournalNucleic acids research
Volume36
Issue numberSUPPL. 1
DOIs
StatePublished - Jan 2008

ASJC Scopus subject areas

  • Genetics

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