V
V. Chandana Epa
Researcher at Commonwealth Scientific and Industrial Research Organisation
Publications - 26
Citations - 2573
V. Chandana Epa is an academic researcher from Commonwealth Scientific and Industrial Research Organisation. The author has contributed to research in topics: Binding site & Insulin receptor. The author has an hindex of 21, co-authored 26 publications receiving 2339 citations.
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Journal ArticleDOI
Quantitative Structure–Property Relationship Modeling of Diverse Materials Properties
TL;DR: Quantitative Structure Property Relationship Modeling of Diverse Materials Properties Tu Le, V. Chandana Epa, Frank R. Burden, and David A. Winkler.
Journal ArticleDOI
Structure of the insulin receptor ectodomain reveals a folded-over conformation
Neil M. McKern,Michael C. Lawrence,Victor A. Streltsov,Meizhen Lou,Timothy E. Adams,George O. Lovrecz,T. C. Elleman,Kim M. Richards,John D. Bentley,Patricia A. Pilling,Peter A. Hoyne,Kellie Cartledge,Tam Pham,Jennifer L. Lewis,Sonia E. Sankovich,Violet Stoichevska,Elizabeth Da Silva,Christine P. Robinson,M. J. Frenkel,Lindsay G. Sparrow,Ross Fernley,V. Chandana Epa,Colin W. Ward +22 more
TL;DR: The structure reveals the domain arrangement in the disulphide-linked ectodomain dimer, showing that the insulin receptor adopts a folded-over conformation that places the ligand-binding regions in juxtaposition, very different from previous models.
Journal ArticleDOI
Ligand-binding properties of a juvenile hormone receptor, Methoprene-tolerant
Jean-Philippe Charles,Thomas Iwema,Thomas Iwema,V. Chandana Epa,Keiko Takaki,Jan Rynes,Marek Jindra +6 more
TL;DR: Results show that Met can sense the JH signal through direct, specific binding, thus establishing a unique class of intracellular hormone receptors.
Journal ArticleDOI
Electrostatic complementarity at protein/protein interfaces.
TL;DR: In this article, a quantitative measure for charge complementarity and electrostatic complementarity was developed and used to investigate protein-protein interfaces in a rigorous manner, and the results demonstrated the relevance of the long-range effects of charges, as described by the electrostatic potential at the binding interface.
Journal ArticleDOI
The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein
Michael C. Lawrence,Patricia A. Pilling,V. Chandana Epa,Anne M. Berry,A. David Ogunniyi,James C. Paton +5 more
TL;DR: The structure of PsaA is the first structure obtained for an ABC-type binding protein from a Gram-positive organism and lacks the characteristic 'hinge peptides' involved in conformational change upon solute uptake and release.