Structure and Function of LIM Domains
Conserved domains found in many proteins provide surfaces that interact with other proteins. Such domains fold independently of the remainder of the protein and are structurally similar within a class of domains. Individual members of a class have sufficient sequence variation to provide high specificity for particular target sequences. Thus, in evolution, conserved structures were retained but variations were selected that provided specific function. Molecular recognition is a fundamental property in biology, long recognized in immunology (antibodies, T and B cell receptors) and in endocrinology (hormone receptors) and more recently appreciated in intracellular signal transduction and transcription processes. Proteins often contain more than one domain either of the same or of a different class that provide for assembly of molecular complexes. The domains discussed in this monograph are in general 40–100 amino acids in length and recognize relatively short but specific sequences in target proteins. In combination, domains and targets constitute a versatile and complex biological language for transfer of information.
KeywordsLymphoma Tyrosine Leukemia Respiration Proline
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