Dr Annette K Shrive
- Title
- Senior Lecturer
- Location
- Huxley Building : 212a
- Role
- Senior Tutor
- Contact me
- Try my office or e-mail to set up an appointment.
- Phone
- +44 (0)1782 733419
- a.k.shrive@keele.ac.uk
Biography
I undertook both my BSc (Physics and Maths) and PhD (Protein Crystallography) at Keele University. The latter involved the development of synchrotron x-ray Laue method for use with large macromolecules such as proteins and viruses. I revisited Keele as a postdoctoral worker and was appointed as a Lecturer at Keele University in September 1999. I have been a visiting scientist at Purdue University, USA and LMB Cambridge and I have undertaken postdoctoral work in structural biology at Keele University, University of Edinburgh and Purdue University, USA.
Research and scholarship
My research interests are in structural biology and in how the structure of biological macromolecules is related to their function and is focused on the structure and function of key molecules of the innate immune system. The innate immune response has non-variable components which respond in a fairly general, often rapid manner to threatening microorganisms and molecules of both internal and external origin. A major focus of my research is on the three-dimensional structures of pentraxins and active fragments of collectins and related proteins and their interactions with natural ligands. Alongside structural work, we also aim to understand how these molecules are functioning in the immune system. From a clinical perspective, one aspect of this work includes analysis of possible modified forms of C-reactive protein in patient serum samples (REC reference 17/WM/0150). Further information on the work of the Structural Biology Research group can be found here.
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Human surfactant protein D |
FIBCD1 with bound ligand |
Human C-reactive protein - Image - T J Greenhough & A K Shrive © Keele University
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Teaching
Year 1
- LSC-10070 Clinical Applications of Biomedical Science
Year 2
- LSC-20015 Molecular, Cellular & Structural Immunology (Module manager)
Year 3
- LSC-30015 Biology of Disease (Module manager)
- LSC-30016 Structural Biology & Macromolecular Function
- LSC-30026 Case Studies in Biomedical Sciences
- LSC-30045 Life Sciences Double Experimental Project
- LSC-30050 Life Sciences Dissertation
Selected Publications
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2020. Monomeric C-Reactive Protein in Serum With Markedly Elevated CRP Levels Shares Common Calcium-Dependent Ligand Binding Properties With an in vitro Dissociated Form of C-Reactive Protein. Frontiers in Immunology, vol. 11. doi> link> full text>
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2019. Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. J Biol Chem, 17155-17165, vol. 294(45). link> doi> full text>
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2018. Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides reveals alternative binding modes for the same LPS. PLoS One, e0199175, vol. 13(6). link> doi> full text>
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2016. Crystal Structure of a Complex of Surfactant Protein D (SP-D) and Haemophilus influenzae Lipopolysaccharide Reveals Shielding of Core Structures in SP-D-Resistant Strains. Infect Immun, 1585-1592, vol. 84(5). link> doi> full text>
Full Publications Listshow
Journal Articles
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2020. Monomeric C-Reactive Protein in Serum With Markedly Elevated CRP Levels Shares Common Calcium-Dependent Ligand Binding Properties With an in vitro Dissociated Form of C-Reactive Protein. Frontiers in Immunology, vol. 11. doi> link> full text>
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2019. Atomic-resolution crystal structures of the immune protein conglutinin from cow reveal specific interactions of its binding site with N-acetylglucosamine. J Biol Chem, 17155-17165, vol. 294(45). link> doi> full text>
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2018. Structural definition of hSP-D recognition of Salmonella enterica LPS inner core oligosaccharides reveals alternative binding modes for the same LPS. PLoS One, e0199175, vol. 13(6). link> doi> full text>
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2016. Crystal Structure of a Complex of Surfactant Protein D (SP-D) and Haemophilus influenzae Lipopolysaccharide Reveals Shielding of Core Structures in SP-D-Resistant Strains. Infect Immun, 1585-1592, vol. 84(5). link> doi> full text>
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2004. C1q and tumor necrosis factor superfamily: modularity and versatility. Trends in Immunology, 551-561, vol. 25(10). doi>
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2004. Structural and functional anatomy of the globular domain of complement protein Clq. Immunology Letters, 113-128, vol. 95(2). doi>
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2004. Isolation and characterization of pentraxin-like serum proteins from the common carp \fICyprinus carpio\fP. Developmental and Comparative Immunology.
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2003. High-resolution Structural Insights into Ligand binding and Immune Cell Recognition by Human Lung Surfactant Protein D. Journal of Molecular Biology.
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2003. Inflammatory interactions in fish exposed to pollutants and parasites:a role for apoptosis and C-reactive protein. Parasitology.
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2003. Comparison of different crystal forms of 3-dehydroquinase from \fISalmonella typhi\fP and its implication for the enzyme activity. Acta Crystallographica, Section D. doi>
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2002. Complete cDNA Sequence of SAP-like Pentraxin from \fILimulus polyphemus\fP:Implications for Pentraxin Evolution. Journal of Molecular Biology.
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2002. The three-dimensional structure of calcium-depleted human C-reactive protein from perfectly twinned crystals. Acta Crystallographica, Section D.
Other
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2011. Structural basis of ligand and pathogen recognition by the collectins. Acta Crystallographica Section A: Foundations of Crystallography (p. C472, vol. A67). doi>
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2011. Structure, function and evolution of the serum pentraxins. Acta Crystallographica Section A: Foundations of Crystallography (p. C546, vol. A67). doi>
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2003. Pentraxin-like serum proteins from common carp \fI(Cyprinus carpio)\fP. Proceedings of the 11th International Conference of the European Association of Fish Pathologists.
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2003. Pentraxin-like serum proteins from common carp \fI(Cyprinus carpio)\fP. Proceedings of the 11th International Conference of the European Association of Fish Pathologists.
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2001. Isolation of C-reactive protein from the common carp \fI(Cyprinius carpio)\fP. Proceedings of the International Conference of the European Association of Fish Pathologists.
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1999. STRUCTURAL COMPARISONS OF TYPE I 3-DEHYDRO-QUINASES. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (p. 287, vol. 55). link>
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1999. STRUCTURE, FUNCTION AND EVOLUTION OF SERUM PENTRAXINS FROM INVERTEBRATES TO HUMANS. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (p. 355, vol. 55). link>
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1999. THE CRYSTAL STRUCTURE OF AN INVERTEBRATE PENTRAXIN-LECTIN WITH A NOVEL MOLECULAR ASSEMBLY. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (p. 197, vol. 55). link>
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1999. THE STRUCTURE OF CALCIUM-DEPLETED HUMAN C-REACTIVE PROTEIN FROM PERFECTLY TWINNED CRYSTALS. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES (p. 350, vol. 55). link>
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X-Ray diffraction data for structure associated with PDB ID: 6ZQY. doi>
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X-Ray diffraction data for structure associated with PDB ID: 6ZR4. doi>
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X-Ray diffraction data relating to protein structure PDB ID: 6RYG. Synchrotron station DLS I03, Diamond Light Source I03.doi>
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X-Ray diffraction data relating to protein structure PDB ID: 6RYM. Synchrotron station SRS 14.1, Daresbury SRS 14.1.doi>
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X-Ray diffraction data relating to protein structure PDB ID: 6RYM. Synchrotron station SRS 14.1, Daresbury SRS 14.1.doi>
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X-ray diffraction data for structure associated with PDB ID: 6ZQR. doi>
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X-ray diffraction data for structure associated with PDB ID: 6ZQX. doi>
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X-ray diffraction data for structure associated with PDB ID: 6ZR0. doi>
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X-ray diffraction data for structure associated with PDB ID: 6ZR3. doi>