(Logo) Domains in Proteins

IndexIndex to Course Material IndexIndex to Section 10 NextIdentification of Domains


Even as the first structures were solved, proteins were found to have structurally distinct lobes (Phillips, 1966). However, the term "domain" was not assigned to compactly folded structures until later when Wetlaufer (1973) recognised it to be a common feature in unrelated proteins. Since then, it has become clear that domains form an important level in the hierarchical organisation of the three-dimensional structure of globular proteins, although not all proteins can be described as multidomain structures.

Domains of recently evolved proteins are frequently encoded by exons, reflecting gene fusion of simpler modules. For example, in the case of hepatocyte growth factors and plasminogens, a number of kringle domains are present.

For a recent review on domain insertion, see Russell (1994). Domain swapping between two protomers is not uncommon (for example in the case of diphtheria toxin (Bennet et al., 1994)).

ALGORITHMS FOR THE IDENTIFICATION OF DOMAINS

Several algorithms for domain identification have been suggested.

Roles of protein domains

-by Stephen D. Rufino, Dept. of Crystallography, Birkbeck College

DOMAIN MOVEMENTS

Domains are important both in protein folding and in biological function. They are found in different combinations and often bring with them discrete functions. The relative disposition of domains in a protein may be important for the function and/or ligand binding. Domain motions are important for a variety of functions.

REFERENCES

There are other useful references in this area.
R.Sowdhamini
IndexIndex to Course Material IndexIndex to Section 10 NextIdentification of Domains

Last updated 11th Jun '96