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Protein structures give disease clues
Date:2/1/2012

nerative diseases.

Calcium also features in a paper published Jan. 23 in the Journal of Biological Chemistry. Ames, David Sacks at the National Institutes of Health, and their colleagues show how a molecule called calmodulin, which is sensitive to calcium, interacts with the estrogen receptor.

When activated with the right amount of calcium, one calmodulin protein attaches to two estrogen receptors and draws them into a bear hug. That structure, or dimer, is then sensitive to the estrogen's attaching to another part of the molecule. In the right amounts, the combination of estrogen, calmodulin and calcium allows the estrogen receptor to attach to DNA and turn particular genes on or off.

The structure also reveals how calmodulin stops the estrogen receptor from being broken down and removed. Another protein, ubiquitin, is responsible for attaching to proteins inside cells and flagging them for disposal. Calmodulin blocks those parts of the estrogen receptor where ubiquitin can attach. That could result in a buildup of estrogen receptors which is associated with tumor formation, Ames said.

X-ray crystallography at the University of Toronto figured in the inositol triphosphate receptor work, while Ames' team used the 800-megahertz nuclear MRI to work on the inositol triphosphate receptor and the calmodulin/estrogen receptor. Similar to the MRI machines used in hospitals, nuclear magnetic resonance spectroscopy provides information about both the structure of molecules and how atoms are moving within them.


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Contact: Andy Fell
ahfell@ucdavis.edu
530-752-4533
University of California - Davis
Source:Eurekalert  

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