DomIns: A Web Resource for Domain
Insertions in Known Protein Structures

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Overview

Domains constitute the structural, functional and evolutionary units of proteins. Proteins can be built from a single domain or an assortment of domains. In naturally occurring multi-domain proteins, the combination almost always occurs end-to-end, i.e., one domain following another domain's C-terminal end. However, there are exceptions to this general pattern, where multi-domain proteins are formed by the insertion of a domain (insert domain) into another domain (parent domain).

We have followed the definition of protein domains as in the SCOP (Structural Classification of Proteins) database to identify domain insertions in known protein structures. Although there are several schemes for protein structure classification, SCOP is central to this work as it is a manually curated classification of proteins of known structures based on their structural and evolutionary relatedness.

We have considered only the major five classes (All-alpha, All-beta, alpha/beta, alpha+beta and Small Proteins), the fold and the superfamily level of SCOP hierarchy for identifying insertions. Apart from browsing insertions in whole PDB, we also provide an option to browse insertions in a pre-computed list of non-redundant PDB chains provided by PDB_Select with a sequence identity threshold of 90%.

Please use the menu in the navigation bar and consult the FAQ page to know more about domain insertion.

We gratefully acknowledge financial support from the Medical Research Council and the Camrbidge Commonwealth Trust.


To report comments and suggestions email aroul@oxfordbiodynamics.com This page was last updated on 17 August 2007