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Title: Crystallographic studies on macrophage inflammatory protein-1α
Author: MacLean, John K. F.
ISNI:       0000 0001 3615 7075
Awarding Body: University of Glasgow
Current Institution: University of Glasgow
Date of Award: 1997
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Macrophage Inflammatory Protein-1alpha is a member of the Chemokine family of inflammatory mediators. In addition to its chemotactic properties, MIP-1alpha is an inhibitor of the proliferation of primitive stem cells, and is therefore potentially useful in cancer therapy. It has also recently been shown to protect certain subsets of human cells from infiltration by HIV-1 virus. The crystal structures of three structural mutants of the Chemokine Macrophage Inflammatory Protein-la have been determined. The structure of a monomeric mutant has been determined to 2.9A, that of a dimeric mutant to 2.3A, and the structure of a tetrameric mutant has been determined in two crystal forms at 2.05A and 1.65A. This thesis outlines the process by which these mutant structures were solved and compares them with other Chemokine structures. The potential implications of the structures of the MIP-1alpha mutants are investigated. The complex network of Chemokines and Chemokine receptors is described, and attempts are made to rationalise receptor-binding specificities of MIP-1alpha and related proteins on the basis of the MIP-1alpha structures.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: Biochemistry