FAQ for Non-Scientists


What is the SGC?

The SGC (Structural Genomics Consortium) is a not-for-profit, public-private partnership with the directive to carry out basic science of relevance to drug discovery. The core mandate of the SGC is to determine 3D structures on a large scale and cost-effectively - targeting human proteins of biomedical importance and proteins from human parasites that represent potential drug targets. In these two areas respectively, the SGC is now responsible for >25% and >50% of all structures deposited into the Protein Data Bank each year; to date (Sep.2011) the SGC has released the structures of over 1200 proteins with implications to the development of new therapies for cancer, diabetes, obesity, and psychiatric disorders.

The SGC is headed by Aled Edwards. Operations at each site are managed by a Chief Scientist - Cheryl Arrowsmith in Toronto, Canada and Chas Bountra in Oxford, UK.

How many people are at the SGC?

The SGC is home to approximately 200 scientists, visiting scientists and other support staff.

Who are the consortium members?

In its third phase, the SGC is funded by 13 separate organizations: AbbVie, Boehringer Ingelheim, the Canada Foundation for Innovation, the Canadian Institutes for Health Research, Genome Canada, GlaxoSmithKline, Janssen, Lilly Canada, the Novartis Research Foundation, the Ontario Ministry of Economic Development and Innovation, Pfizer, Takeda, and the Wellcome Trust.

What are the rights of consortium members?

For a donation of 8 Million US dollars, an organization gains the following rights.

  1. The right to nominate targets to the Target List
  2. The right to nominate a member to the Scientific Committee and the Board of Directors
  3. The right to place scientists to work within the SGC laboratories, under a confidentiality agreement.

What is a protein?

Proteins are biological molecules. There are more than 20,000 different proteins in the human body. The instructions for how to make a protein are coded in our DNA, within parts called genes. Protein is also a collective name; this is the term that is used in nutrition to describe what we eat. Proteins serve many purposes in the body. Proteins such as keratin and collagen are the main ingredients in your hair, muscles, tendons and skin and help give structure to the body. Amylase is a protein that helps your body digest starch, hemoglobin is responsible for transporting oxygen in the blood stream, insulin helps regulate the storage of glucose in the body and the list goes on and on. Because proteins have different functions, they also have different shapes. To date, we know the shapes of about 10% of the proteins in the human body.

Why is finding out the shapes of human proteins important?

Because proteins perform many of the essential functions in the human body, it is not surprising that when we get sick, it is often as a result of a protein, or a group of proteins, failing to act in their normal way. Most medicines work by binding to proteins and influencing their activity. For example, cyclooxygenase is a protein that produces signals that caused swelling and pain in response to injury. Aspirin binds to this protein and stops it from working, and therefore reduces the pain and swelling. To work effectively, medicines must find the right protein, like a key in a lock. Knowing the shape of a protein "target" enables drug discovery researchers to design drugs with molecules that "fit." When used effectively, the structure of a protein drug target can speed up the discovery of new medicines by 18 months or more.

What is structural genomics?

It is very expensive to determine a new protein structure, as much as one million dollars. However, with improvements in methods, computers and with access to the complete sequence of our DNA (the human genome), it is possible to adopt more systematic approaches, and thus reduce the time and cost to determine the shapes of proteins. Structural genomics aims to determine the three-dimensional structures of proteins at a rapid rate and in a cost-effective manner. Structural information provides one of the most powerful means to discover how the protein works. It provides the diagram that others can use to write the user's manual.

Are any outside groups (ie. collaborators, funders) able to see the results prior to being released to the public?

No. The structural information is made available to everyone either when the structure is released by the PDB, or pre-released on www.thesgc.org.

Why release your research into the public domain?

The structures of human proteins in essence is part of the information that defines what it is to be human. Because of the fundamental nature and importance of the information, we place our results immediately and without restriction into the public domain. This not only provides the public with this fundamental knowledge, but also allows commercial efforts and other academics to utilize the data freely and without any delay.

"What society wants," says the SGC's CEO, Dr. Aled Edwards, "is for all this information to be out there, free of charge, no patents, no restrictions. And that's what we do." The result is greater knowledge about the human body and about the mechanisms of disease. The information also promotes faster drug discovery, bringing potentially life-saving drugs to market sooner and more cheaply.

Do all SGC sites work on the same projects?

Each geographical site works on a number of different protein families. All sites focus on primarily on human proteins.

What is the PDB?

The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. This data is submitted by biologists and biochemists from around the world and is released into the public domain, and can be accessed for free.

What is PubMed?

PubMed is a free search engine which searches the MEDLINE database of citations and abstracts of biomedical research articles. Although the key subject is medicine, and its related fields, it also provides very comprehensive coverage of the related biomedical sciences, such as biochemistry and cell biology. PubMed covers over 5,000 journals published in the United States and more than 80 other countries primarily from 1950 to the present.

Who decides which proteins become SGC targets?

The SGC must determine a pre-defined number of structures of proteins from a Target List created by its funders and approved by the SGC Scientific Committee. The Target List comprises proteins selected not for perceived technical ease, but rather for relevance to human health and disease. The Target List comprises proteins selected by both academic and participating industrial researchers, and thus contains information that could potentially be used to commercial advantage. As a result, the SGC maintains the Target List as confidential information; neither consortium members nor the public are aware of the proteins on the Target List (the consortium members are, of course, aware of the proteins that they nominated for the Target List).

Normally only new structures of human or parasite are counted towards the SGC goals; however, in the interest of understanding issues such as enzyme function, selectivity and specificity, certain follow-up structures (such as protein-ligand complexes) may also be counted. These follow-on structures are reviewed by the SGC Scientific Committee on a case-by-case basis and are approved as counted structures for cases in which the additional structure has significant impact on the understanding of the protein function or mechanism of action/inhibition. Such follow-on structures are limited to no more than 10% of the total output.

Are there other groups like the SGC working on the same set of proteins?

Due to the central importance of the proteins on the SGC Target List, it is likely that many of the proteins that are being pursued by the SGC are also being pursued in academia and in industry. The SGC hopes that by immediately releasing the structural information, the reagents and the methods, it will facilitate the research efforts of these groups.

Who do I contact if I am interested in collaborating with SGC?

The SGC is highly committed to rapid dissemination of its research results through collaboration with the scientific community.

Our scientists work with others around the globe to

  • elucidate the functional implications of our structures and protein targets in general,
  • screen our protein targets against our collaborators' focused or diverse libraries,
  • take advantage of external expertise to characterize the activity of our proteins,
  • extend our understanding of our protein families of interest, and collaborate on expressing our proteins and reaching structural solutions more expediently.

Contact us to initiate discussion on potential collaboration on our structures.

Is it possible to spend time within the SGC to work on collaborative targets?

Yes. The SGC has a visiting scientist program in which external scientists, graduate students and postdoctoral fellows who have a position at another institution are invited to work within the SGC on proteins of mutual interest. These collaborations are undertaken under the following terms:

  • 6-12 month terms at an SGC site
  • Individuals are expected to cover their own salary and local accommodations.
  • Individuals would be expected to work on SGC target proteins with the goal of obtaining a 3D structure. Examples of potential projects include expression, purification, crystallization and structure determination of proteins; biochemical and structural chracterization of protein-protein or protein-small molecule interactions; structure determination of SNP variants.
  • Individuals are required to sign confidentiality agreement
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