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DomIns: a web resource for domain insertions in known protein structures.

ABSTRACT: Proteins can be formed by single or multiple domains. The process of recombination at the molecular level has generated a wide variety of multi-domain proteins with specific domain organization to cater to the functional requirements of an organism. The functional and structural costs of inserting a domain into another means that multi-domain proteins are usually formed by covalently linking the N-terminus of one domain to the C-terminus of the preceding domain. While this is true in a large proportion of multi-domain proteins, we find a significant fraction of proteins that are the result of domain insertion. The inserted domain breaks the sequence contiguity of the domain into which it is inserted leading to a novel domain organization. This web resource aims to document domain insertions in known protein structures that are classified in the SCOP database. The web server can be accessed from http://stash.mrc-lmb.cam. ac.uk/DomIns/.

SUBMITTER: Selvam RA

PROVIDER: S-EPMC308781 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature

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DomIns: a web resource for domain insertions in known protein structures.

Selvam R Aroul RA Sasidharan Rajkumar R

Nucleic acids research 20040101 Database issue

Proteins can be formed by single or multiple domains. The process of recombination at the molecular level has generated a wide variety of multi-domain proteins with specific domain organization to cater to the functional requirements of an organism. The functional and structural costs of inserting a domain into another means that multi-domain proteins are usually formed by covalently linking the N-terminus of one domain to the C-terminus of the preceding domain. While this is true in a large pro ...[more]

PMID: 14681392

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