The GxxxG motif: a framework for transmembrane helix-helix association

WP Russ, DM Engelman - Journal of molecular biology, 2000 - Elsevier
In order to identify strong transmembrane helix packing motifs, we have selected transmembrane
domains exhibiting high-affinity homo-oligomerization from a randomized sequence …

Evolutionary information for specifying a protein fold

M Socolich, SW Lockless, WP Russ, H Lee… - Nature, 2005 - nature.com
Classical studies show that for many proteins, the information required for specifying the
tertiary structure is contained in the amino acid sequence. Here, we attempt to define the …

TOXCAT: a measure of transmembrane helix association in a biological membrane

WP Russ, DM Engelman - Proceedings of the National …, 1999 - National Acad Sciences
The noncovalent association of transmembrane α-helices is a fundamental event in the folding
of helical membrane proteins. In this work, a system (TOXCAT) is developed for the study …

Interhelical hydrogen bonding drives strong interactions in membrane proteins

F Xiao Zhou, MJ Cocco, WP Russ, AT Brunger… - Nature structural …, 2000 - nature.com
Polar residues in transmembrane α-helices may strongly influence the folding or association
of integral membrane proteins. To test whether a motif that promotes helix association in a …

Surface sites for engineering allosteric control in proteins

…, M Natarajan, VC Nashine, M Socolich, T Vo, WP Russ… - Science, 2008 - science.org
Statistical analyses of protein families reveal networks of coevolving amino acids that
functionally link distantly positioned functional surfaces. Such linkages suggest a concept for …

An evolution-based model for designing chorismate mutase enzymes

WP Russ, M Figliuzzi, C Stocker, P Barrat-Charlaix… - Science, 2020 - science.org
The rational design of enzymes is an important goal for both fundamental and practical
reasons. Here, we describe a process to learn the constraints for specifying proteins purely from …

Natural-like function in artificial WW domains

WP Russ, DM Lowery, P Mishra, MB Yaffe… - Nature, 2005 - nature.com
Protein sequences evolve through random mutagenesis with selection for optimal fitness 1 .
Cooperative folding into a stable tertiary structure is one aspect of fitness, but evolutionary …

An interdomain sector mediating allostery in Hsp70 molecular chaperones

RG Smock, O Rivoire, WP Russ, JF Swain… - Molecular systems …, 2010 - embopress.org
Allosteric coupling between protein domains is fundamental to many cellular processes. For
example, Hsp70 molecular chaperones use ATP binding by their actin‐like N‐terminal …

An electrostatic selection mechanism controls sequential kinase signaling downstream of the T cell receptor

…, D Karandur, TA Kadlecek, IR Fallahee, WP Russ… - Elife, 2016 - elifesciences.org
10.7554/eLife.20105.001 The sequence of events that initiates T cell signaling is dictated by
the specificities and order of activation of the tyrosine kinases that signal downstream of the …

Saturation mutagenesis of α-synuclein reveals monomer fold that modulates aggregation

J Chlebowicz, W Russ, D Chen, A Vega, S Vernino… - Science …, 2023 - science.org
α-Synuclein (aSyn) aggregation underlies neurodegenerative synucleinopathies. aSyn seeds
are proposed to replicate and propagate neuronal pathology like prions. Seeding of aSyn …