Linkers in the structural biology of protein–protein interactions

VP Reddy Chichili, V Kumar, J Sivaraman - Protein science, 2013 - Wiley Online Library
Linkers or spacers are short amino acid sequences created in nature to separate multiple
domains in a single protein. Most of them are rigid and function to prohibit unwanted …

Grading the commercial optical biosensor literature—Class of 2008:'The Mighty Binders'

RL Rich, DG Myszka - Journal of Molecular Recognition: An …, 2010 - Wiley Online Library
Optical biosensor technology continues to be the method of choice for label‐free, real‐time
interaction analysis. But when it comes to improving the quality of the biosensor literature …

Conformational changes and flexibility in T-cell receptor recognition of peptide–MHC complexes

KM Armstrong, KH Piepenbrink… - Biochemical Journal, 2008 - portlandpress.com
A necessary feature of the immune system, TCR (T-cell receptor) cross-reactivity has been
implicated in numerous autoimmune pathologies and is an underlying cause of transplant …

RosettaBackrub—a web server for flexible backbone protein structure modeling and design

F Lauck, CA Smith, GF Friedland… - Nucleic acids …, 2010 - academic.oup.com
Abstract The RosettaBackrub server (http://kortemmelab. ucsf. edu/backrub) implements the
Backrub method, derived from observations of alternative conformations in high-resolution …

Structural and dynamic control of T‐cell receptor specificity, cross‐reactivity, and binding mechanism

BM Baker, DR Scott, SJ Blevins… - Immunological …, 2012 - Wiley Online Library
Over the past two decades, structural biology has shown how T‐cell receptors engage
peptide/major histocompatibility complex (MHC) complexes and provided insight into the …

Disparate degrees of hypervariable loop flexibility control T-cell receptor cross-reactivity, specificity, and binding mechanism

DR Scott, OY Borbulevych, KH Piepenbrink… - Journal of molecular …, 2011 - Elsevier
αβ T-cell receptors (TCRs) recognize multiple antigenic peptides bound and presented by
major histocompatibility complex molecules. TCR cross-reactivity has been attributed in part …

T cells and their eons‐old obsession with MHC

L Yin, J Scott‐Browne, JW Kappler… - Immunological …, 2012 - Wiley Online Library
T cells bearing receptors made up of α and β chains (TCR s) usually react with peptides
bound to major histocompatibility complex proteins (MHC). This bias could be imposed by …

Structural features of T cell receptor variable regions that enhance domain stability and enable expression as single-chain VαVβ fragments

SA Richman, DH Aggen, ML Dossett… - Molecular …, 2009 - Elsevier
The variable (V) domains of antibodies and T cell receptors (TCRs) share sequence
homology and striking structural similarity. Single-chain antibody V domain constructs (scFv) …

Thermodynamics of T‐cell receptor–peptide/MHC interactions: progress and opportunities

KM Armstrong, FK Insaidoo… - Journal of Molecular …, 2008 - Wiley Online Library
Abstract αβ T‐cell receptors (TCRs) recognize peptide antigens presented by class I or class
II major histocompatibility complex molecules (pMHC). Here we review the use of …

Examining variable domain orientations in antigen receptors gives insight into TCR-like antibody design

J Dunbar, B Knapp, A Fuchs, J Shi… - PLoS computational …, 2014 - journals.plos.org
The variable domains of antibodies and T-Cell receptors (TCRs) share similar structures.
Both molecules act as sensors for the immune system but recognise their respective …