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Your search keyword '"Reid, Kenneth B. M."' showing total 13 results
Start Over Author "Reid, Kenneth B. M." Journal biochemistry
13 results on '"Reid, Kenneth B. M."'

1. Role of Ca(super 2+) in the electrostatic stability and the functional activity of the globular domain of human Clq

Author

Roumenina, Lubka T., Reid, Kenneth B. M., Kantatdjiev, Alexandar A., Mantovani, Alberto, Atanasov, Boris P., Kishor, Uday, Waters, Patrick, Kojouharova,Mihaela S., and Gadjeva, Mihaela

Subjects
Globular proteins -- Chemical properties, Electrostatics -- Analysis, Calcium ions -- Chemical properties, Biological sciences, Chemistry
Abstract

The role of Ca(super 2+) in the electrostatic stability and target-binding properties of the native Clq and the recombinant monomeric forms of the globular head domain (gClq) of human Clq are investigated using theoretical and experimental approaches. It is concluded that Ca(super 2+) primarily influences the target recognition properties of Clq and the loss of Ca(super 2+) at pH 7.4 leads to change in the direction of electric moment which is important for subsequent complement activation.

Published
2005

3. Existence of Different but Overlapping IgG- and IgM-Binding Sites on the Globular Domain of Human C1q

Author

Zlatarova, Alexandra S., primary, Rouseva, Marieta, additional, Roumenina, Lubka T., additional, Gadjeva, Mihaela, additional, Kolev, Martin, additional, Dobrev, Ivan, additional, Olova, Neli, additional, Ghai, Rohit, additional, Jensenius, Jens Chr., additional, Reid, Kenneth B. M., additional, Kishore, Uday, additional, and Kojouharova, Mihaela S., additional

Published
2006
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4. Interaction of C1q with IgG1, C-reactive Protein and Pentraxin 3: Mutational Studies Using Recombinant Globular Head Modules of Human C1q A, B, and C Chains

Author

Roumenina, Lubka T., primary, Ruseva, Marieta M., additional, Zlatarova, Alexandra, additional, Ghai, Rohit, additional, Kolev, Martin, additional, Olova, Neli, additional, Gadjeva, Mihaela, additional, Agrawal, Alok, additional, Bottazzi, Barbara, additional, Mantovani, Alberto, additional, Reid, Kenneth B. M., additional, Kishore, Uday, additional, and Kojouharova, Mihaela S., additional

Published
2006
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13. Role of Ca2+ in the electrostatic stability and the functional activity of the globular domain of human C1q.

Author

Roumenina LT, Kantardjiev AA, Atanasov BP, Waters P, Gadjeva M, Reid KB, Mantovani A, Kishore U, and Kojouharova MS

Subjects
Calcium chemistry, Cations, Divalent, Complement C1q metabolism, Enzyme-Linked Immunosorbent Assay, Humans, Hydrogen-Ion Concentration, Immunoglobulin G chemistry, Immunoglobulin G metabolism, Immunoglobulin M chemistry, Immunoglobulin M metabolism, Immunoglobulins metabolism, Protein Binding, Protein Conformation, Static Electricity, Calcium metabolism, Complement C1q chemistry, Immunoglobulins chemistry
Abstract

C1q is the recognition subunit of the classical pathway of the complement system and a major connecting link between classical pathway-driven innate immunity and IgG- or IgM-mediated acquired immunity. The basic structural subunit of C1q is composed of an N-terminal triple-helical collagen-like region and a C-terminal heterotrimeric globular head domain (gC1q) that is made up of individual A, B, and C chains. Recent crystallographic studies have revealed that the gC1q domain, which is the main target-binding region of C1q, has a compact and spherical heterotrimeric assembly, held together by both electrostatic and nonpolar interactions, with quasi-3-fold symmetry. A characteristic feature of the gC1q domain is the presence of a exposed Ca(2+) located near the apex. We have investigated, using theoretical and experimental approaches, the role of Ca(2+) in the electrostatic stability and target-binding properties of the native C1q as well as recombinant monomeric forms of the C-terminal regions of the A, B, and C chains. Here, we report that Ca(2+) primarily influences the target recognition properties of C1q toward IgG, IgM, C-reactive protein, and pentraxin 3. At pH 7.4, the loss of Ca(2+) leads to changes in the direction of electric moment from coaxial (where the putative C-reactive protein-binding site is located) to perpendicular to the molecular axis (toward the most likely IgG-binding site), which appears important for target recognition by C1q and subsequent complement activation.

Published
2005
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