Research Topics
Genomes and Genes | Ioannis VakonakisSummaryAffiliation: University of Oxford Country: UK Publications
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Publications
Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domainIoannis Vakonakis
Department of Biochemistry, University of Oxford, South Parks Road, Oxford, United Kingdom
Structure 16:944-53. 2008..We postulate that this domain class facilitates direct protein-protein interactions in many transmembrane receptors...- Motogenic sites in human fibronectin are masked by long range interactionsIoannis Vakonakis
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK
J Biol Chem 284:15668-75. 2009..Anastellin, which promotes fibril formation, destabilizes (3)FnIII and disrupts the observed (4-5)FnI-(3)FnIII interaction. We discuss these findings in the context of the control of cellular activity through exposure of masked sites... - Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnIMichele C Erat
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, Germany
J Biol Chem 285:33764-70. 2010..We explore the implications of this model using long collagen peptides and discuss our findings in the context of FN interactions with collagen fibrils... - Identification and structural analysis of type I collagen sites in complex with fibronectin fragmentsMichele C Erat
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom
Proc Natl Acad Sci U S A 106:4195-200. 2009..We demonstrate, by kinetic unfolding experiments, that the triple-helical collagen state is destabilized by (8-9)FnI. This finding suggests a role for fibronectin in collagen proteolysis and tissue remodeling... - Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesisIoannis Vakonakis
The Department of Biochemistry, University of Oxford, Oxford, UK
EMBO J 26:2575-83. 2007..We speculate on the importance of this interaction for FN function and present a possible mechanism by which tension could initiate fibrillogenesis... - The structure of an integrin/talin complex reveals the basis of inside-out signal transductionNicholas J Anthis
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
EMBO J 28:3623-32. 2009..These results show key structural features that explain the ability of talin to mediate inside-out TM signalling... - Structural analysis of the interactions between paxillin LD motifs and alpha-parvinSonja Lorenz
Laboratory of Molecular Biophysics, University of Oxford, Oxford OX1 3QU, United Kingdom
Structure 16:1521-31. 2008..Taken together, these results reveal an unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell... - Extracellular matrix: from atomic resolution to ultrastructureIoannis Vakonakis
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK
Curr Opin Cell Biol 19:578-83. 2007..Emphasis is placed on the key role of intermolecular interactions in assembling larger, microm scale, structures... - An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin bindingCamilla L Oxley
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
J Biol Chem 283:5420-6. 2008..This switch may represent an in vivo mechanism for control of integrin receptor activation. These results have implications for the control of integrin signaling by proteins containing phosphotyrosine binding domains... - Latrophilin signaling links anterior-posterior tissue polarity and oriented cell divisions in the C. elegans embryoTobias Langenhan
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK
Dev Cell 17:494-504. 2009..We dissect the molecular requirements of lat-1 signaling and implicate lat-1 in an anterior-posterior tissue polarity pathway in the premorphogenesis stage of C. elegans development... - Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitopeChristina Mayer
Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom
J Biol Chem 287:7182-9. 2012..We propose that PHIST domains facilitate protein interactions, and that the conserved ATS epitope may be targeted to disrupt the parasite cytoadherence system... - Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanismStanly B Williams
Department of Biology, Texas A and M University, College Station 77843, USA
Proc Natl Acad Sci U S A 99:15357-62. 2002..We propose that this pseudo-receiver is a timing input-device that regulates KaiA stimulation of KaiC autophosphorylation, which in turn is essential for circadian timekeeping... - Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasAIoannis Vakonakis
Department of Biochemistry and Biophysics, Texas A and M University, College Station 77843, USA
J Mol Biol 342:9-17. 2004..We suggest that this surface is used by N-SasA for protein-protein interactions. Our analysis suggests that the structural differences between N-SasA and KaiB are the result of only a few critical amino acid substitutions... - Crystal structure of circadian clock protein KaiA from Synechococcus elongatusSheng Ye
Center for Structural Biology, Institute of Biosciences and Technology, Houston, TX 77030, USA
J Biol Chem 279:20511-8. 2004..The structure suggests that the KaiB binding site is covered in the dimer interface of the KaiA "closed" conformation, observed in the crystal structure, which suggests an allosteric regulation mechanism... - Sequence-specific 1H, 13C and 15N resonance assignments of the C-terminal domain of KaiA, a circadian clock proteinIoannis Vakonakis
J Biomol NMR 28:403-4. 2004 - NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interactionIoannis Vakonakis
Departments of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843, USA
Proc Natl Acad Sci U S A 101:1479-84. 2004..This NMR structure and a 21-A-resolution electron microscopy structure of the hexameric KaiC particle allow us to postulate a mode of KaiA-KaiC interaction, in which KaiA binds a linker region connecting two globular KaiC domains...