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The Crystal Structure of the Globular Head of Complement Protein C1q Provides a Basis for Its Versatile Recognition Properties*
- C. Gaboriaud, J. Juanhuix, G. Arlaud
- Chemistry, BiologyJournal of Biological Chemistry
- 21 November 2003
The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to 1.9 Å of resolution, revealing a compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions.
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
It is postulate that only the A-clusters containing two Ni ions are catalytically active in the tetrameric α2β2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica.
C1q Binds Phosphatidylserine and Likely Acts as a Multiligand-Bridging Molecule in Apoptotic Cell Recognition1
Data suggest that C1q has the unique ability to sense different markers which collectively would provide strong eat me signals, thereby allowing efficient apoptotic cell removal.
CDR3 loop flexibility contributes to the degeneracy of TCR recognition
Crystal structure determination showed that the BM3.3 TCR complementarity-determining region (CDR) 3α could undergo rearrangements to adapt to structurally different peptide residues, which helps explain TCR binding cross-reactivity.
A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex.
Crystal structure of a T cell receptor bound to an allogeneic MHC molecule
The results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-M HC molecules.
X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli
- A. Volbeda, P. Amara, J. Fontecilla-Camps
- ChemistryProceedings of the National Academy of Sciences
- 19 March 2012
The crystal structure of the membrane-bound O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli (EcHyd-1) has been solved in three different states: as-isolated, H2-reduced, and chemically…
Crystal structure of human iron regulatory protein 1 as cytosolic aconitase.
Crystal structure of the O(2)-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome b.
Structural basis of X-ray-induced transient photobleaching in a photoactivatable green fluorescent protein.
- V. Adam, P. Carpentier, D. Bourgeois
- ChemistryJournal of the American Chemical Society
- 1 December 2009
The combined X-ray diffraction and in crystallo UV-vis absorption, fluorescence, and Raman data reveal that radical formation in IrisFP involves pronounced but reversible distortion of the chromophore, suggesting a transient loss of pi conjugation.