ProfessorKurt Drickamer
Chair in Biochemistry
Department of Life Sciences - Faculty of Natural Sciences
Orcid identifier0000-0001-5026-5996 (opens in a new tab)
- Chair in BiochemistryDepartment of Life Sciences - Faculty of Natural Sciences
- 020 7594 5282 (Work)
- 606, Sir Ernst Chain Building, South Kensington Campus, United Kingdom
BIO
Molecular function of sugar-binding receptors in cellular recognition events
Specific arrangements of sugars decorate the surfaces of cells and are attached to proteins released from cells into the circulation and other extracellular spaces. These glycans serve as recognition signals that are bound by special receptors. In animals, many of these receptors bind to endogenous carbohydrate structures, forming the basis for cell-cell adhesion and for the selective removal of proteins from circulation. Other receptors bind foreign carbohydrates on the surfaces of potentially pathogenic micro-organisms and form part of the innate, antibody-independent immune system. Many sugar-binding receptors contain related carbohydrate-recognition domains and mutations in some of these proteins are associated with susceptibility to disease.This research is a joint project with Dr Maureen Taylor, who is also in the Division of Molecular Biosciences. A combination of biochemical, biophysical and molecular biological approaches allows us to understand how carbohydrate-recognition domains work together to provide selective recognition of glycoproteins and cell surfaces. We also seek to determine how such recognition leads to targeting of biological functions such as complement fixation and how genetic variation in sugar-binding receptors causes changes in their molecular properties and hence contributes to human disease. In addition, our knowledge of the structure and function of carbohydrate-recognition domains can be combined with the results of the human and model organism genome projects to identify novel sugar-binding receptors and thus to develop a broader understanding of the biological roles of sugar recognition.
Link to the Genomic Resource for Animal Lectins.
Specific arrangements of sugars decorate the surfaces of cells and are attached to proteins released from cells into the circulation and other extracellular spaces. These glycans serve as recognition signals that are bound by special receptors. In animals, many of these receptors bind to endogenous carbohydrate structures, forming the basis for cell-cell adhesion and for the selective removal of proteins from circulation. Other receptors bind foreign carbohydrates on the surfaces of potentially pathogenic micro-organisms and form part of the innate, antibody-independent immune system. Many sugar-binding receptors contain related carbohydrate-recognition domains and mutations in some of these proteins are associated with susceptibility to disease.This research is a joint project with Dr Maureen Taylor, who is also in the Division of Molecular Biosciences. A combination of biochemical, biophysical and molecular biological approaches allows us to understand how carbohydrate-recognition domains work together to provide selective recognition of glycoproteins and cell surfaces. We also seek to determine how such recognition leads to targeting of biological functions such as complement fixation and how genetic variation in sugar-binding receptors causes changes in their molecular properties and hence contributes to human disease. In addition, our knowledge of the structure and function of carbohydrate-recognition domains can be combined with the results of the human and model organism genome projects to identify novel sugar-binding receptors and thus to develop a broader understanding of the biological roles of sugar recognition.
Link to the Genomic Resource for Animal Lectins.
FACULTY
- Faculty of Natural Sciences
POSITION NAME
- Chair in Biochemistry