5. October 2007
Important protein structure determinedMedia Releases Biology Research Using Synchrotron Light
CAP-Gly domains control fundamental cellular processes
Using biochemical, cell biological and biophysical information including X-ray crystallographic data collected at the Swiss Light Source (SLS) researchers at PSI, in collaboration with groups in Rotterdam and University of Zürich, now unraveled the molecular basis of CAP-Gly domain function which turned out to be conserved from yeast to man. Their findings further offer a basis for understanding the origin of hypoparathyroidism-retardation-dismorphysm and distal spinal muscular atrophy, two hereditary human diseases. The results were recently published in the renowned journal Nature Structural and Molecular Biology (Volume 14, No 10, pp. 959 - 967).
Many biological processes are controlled by the interaction of protein molecules within cells. These proteins often consist of module-like building blocks. One of these protein modules is the so-called CAP-Gly domain, which was discovered in 1993. Despite the implication of CAP-Gly domains in fundamental cellular processes such as cell division, cell migration and intracellular organelle and vesicle transport the underlying mechanism of their actual functions remained poorly understood.
NSMB Paper Structure-function relationship of CAP-Gly domains (Download PDF)