Xiaojing Yang
University of Illinois Chicago, IL·Biophysics
Cells constantly sense their surroundings and pass signals inward. Many do this with receptor kinases, proteins that detect a trigger such as light or a chemical and then attach phosphate groups to pass the signal on.
- Fields
Biophysics
Biochemistry
Chemistry
- Topics
photoreceptors
receptor kinases
histidine kinases
- Grants
- 1 known grant, through May 2029
What they work on
- Determine full-length cryo-EM structures of a bacteriophytochrome and a dual-sensor photoreceptor kinase in different signaling states by resolving structural heterogeneity, meaning the mix of shapes the proteins adopt.
- Test the functional relevance of the resolved structures by comparing how common each shape is in cryo-EM datasets collected under different light and ligand conditions.
- Analyze motions of the central helical spine, dimer asymmetry and order-disorder transitions in long-range signaling, combining cryo-EM and crystallography.
- Probe the key interactions behind allosteric regulation and signal integration in these light-activated kinases, using mutagenesis and functional assays.
More about the research
How sensing at one end of the protein switches on activity at the other end, a process called allostery, is still poorly understood. These proteins are flexible, so structural studies have mostly used cut-down fragments rather than the whole protein.
Why it matters
Receptor kinases are central to disease biology and drug discovery. Clarifying how they switch on could reveal general rules of protein allostery. Light-switchable bilin photoreceptors could also serve as a basis for optogenetic tools, which use light to control cells. In the long run, this may help engineer light-activated enzymes for research and new therapeutic strategies.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Lan Zhu
Medical College of Wisconsin, WI·Biophysics
Determine the structures of non-Class B GPCRs bound to receptor activity-modifying proteins (RAMPs) using cryo-EM, crystallography, and molecular dynamics, to learn how RAMPs control surface localization and ligand recognition.
James Solomon Fraser
University of California-San Francisco, CA·Biophysics
Improve computational methods for finding and modeling alternative protein shapes in cryoEM density maps, extending the multiconformer modeling the group built for X-ray crystallography.
James Chen
University of California-San Francisco, CA·Biophysics·Early-career
Purify the cell-wall proteins PonA1 and CrgA and their partner complexes directly from Mycobacterium tuberculosis and M. smegmatis, and determine their 3D structures by single-particle cryo-EM.
The school
University of Illinois Chicago: 42 labs on PI Pages, $532M a year on research, 359 research doctorates a year.
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