Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.596466
Title: Evolution of the structure and function of the immunoglobulin superfamily
Author: Bateman, A. G.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 1997
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Abstract:
Structure and sequence can be used to trace the evolution of a protein domain over the course of several hundred million years. Here it is shown that the immunoglobulin I-set is present in sub-vertebrates, whereas the C1, C2, V and I-sets are found in vertebrates. This implies that the I-set is the ancestral set and that the Cl, C2 and V-sets arose from I-set ancestors. The I-set arose at least 800 million years ago, and the C1, C2 and V-sets diverged from the I-set some 400 million years ago. Phylogenetic analysis of immunoglobulin kinases shows that they have arisen by at least two independent associations with immunoglobulin-like domains, once with receptor tyrosine kinases and once with intracellular serine/threonine muscle kinases. Prokaryotic examples of the immunoglobulin superfamily are discovered in two bacterial proteins and a bacteriophage T4 protein. These are probably the products of horizontal transmission from animals. Outline structures for the extracellular immunoglobulin-like domains of fibroblast growth factor receptor and the L1 cell adhesion molecule are presented. These outline structures describe the relative positions of residues in the domains, their major secondary structures and gives a guide to the extent residues are accessible to the solvent. These outline structures are used to provide molecular explanations for mutations that lead to human disease. All proteins contain key residue sites and mutations at these sites will disrupt structure, reduce stability and in some cases alter the conformation of functional sites. The majority of mutations in fibroblast growth factor receptors and L1 occur at key residue sites. In myelin protein zero, an immunoglobulin disease protein of known structure, the majority of mutations occur in, or near, functional sites.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.596466  DOI: Not available
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