Structural highlights
Function
LNX2_HUMAN
Publication Abstract from PubMed
The internal mechanics of proteins-the coordinated motions of amino acids and the pattern of forces constraining these motions-connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2PDZ2) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function.
Electric-field-stimulated protein mechanics.,Hekstra DR, White KI, Socolich MA, Henning RW, Srajer V, Ranganathan R Nature. 2016 Dec 15;540(7633):400-405. doi: 10.1038/nature20571. Epub 2016 Dec 7. PMID:27926732[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hekstra DR, White KI, Socolich MA, Henning RW, Srajer V, Ranganathan R. Electric-field-stimulated protein mechanics. Nature. 2016 Dec 15;540(7633):400-405. doi: 10.1038/nature20571. Epub 2016 Dec 7. PMID:27926732 doi:http://dx.doi.org/10.1038/nature20571
