A new ‘Periodic Table’ provides a unified way to classify and visualize Protein Complexes

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Periodic Table of Protein Complexes | EMBL-EBI

The study provides insights into evolutionary distribution of different types of existing protein complexes. The table provides a valuable tool for biotechnology and the engineering of novel complexes.

Almost every biological process depends on proteins interacting and assembling into complexes in a specific way, and many diseases are associated with problems in complex assembly. The principles underpinning this organisation are not yet fully understood, but by defining the fundamental steps in the evolution of protein complexes, the new ‘periodic table’ presents a systematic, ordered view on protein assembly, providing a visual tool for understanding biological function.

“Evolution has given rise to a huge variety of protein complexes, and it can seem a bit chaotic,” explains Joe Marsh. “But if you break down the steps proteins take to become complexes, there are some basic rules that can explain almost all of the assemblies people have observed so far.”

Protein complex assembly can be seen as endless variations on dimerization (1 doubles, and becomes 2), cyclisation (1 forms a ring of 3 or more) and subunit addition (2 different proteins bind to each other). Because these happen in a fairly predictable way, it’s not as hard as you might think to predict how a novel protein would form.

“What we’ve made is a classification based on these underlying principles that helps people get a handle on the complexity.” The exceptions to the rule are interesting in their own right, adds Sebastian Ahnert, as are the subject of on-going studies.

“By analysing the tens of thousands of protein complexes for which 3D structures have already been experimentally determined, we could see repeating patterns in the assembly transitions that occur – and with new data from mass spectrometry we could start to see the bigger picture,” says Joe.

“The core work for this study is in theoretical physics and computational biology, but it couldn’t have been done without the mass spectrometry work by our colleagues at Oxford University,” adds Sarah Teichmann, Research Group Leader at EMBL-EBI and Wellcome Trust Sanger Institute. “This is yet another excellent example of how extremely valuable interdisciplinary research can be.” http://www.ebi.ac.uk/about/news/press-releases/periodic-table-protein-complexes