Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains.

ABSTRACT: Compilations of domain-domain interactions based on solved structures suggest there are distinct domain pairs that are used repeatedly in different protein contexts to mediate protein-protein interactions. However, not all protein pairs with the corresponding domains that can potentially mediate interaction do interact, even when they are colocalized and coexpressed. It is conceivable that there are structural and sequence features, below the domain level, that play a role in determining the potential of domains to mediate protein-protein interactions. Here, we discover such features by comparing domains that, on the one hand, mediate homodimerization of proteins and, on the other, occur in different proteins that are documented as monomers. Intriguingly, this comparison uncovered surface

SUBMITTER: Akiva E 

PROVIDER: S-EPMC2533183 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature