International
Tables for
Crystallography
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 1.3, p. 25   | 1 | 2 |

Section 1.3.6. Outlook and dreams

W. G. J. Hola* and C. L. M. J. Verlindea

aBiomolecular Structure Center, Department of Biological Structure, Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195-7742, USA
Correspondence e-mail:  hol@gouda.bmsc.washington.edu

1.3.6. Outlook and dreams

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At the beginning of the 1990s, Max Perutz inspired many researchers with a passion for structure and a heart for the suffering of mankind with a fascinating book entitled Protein Structure – New Approaches to Disease and Therapy (Perutz, 1992[link]). The explosion of medicinal macromolecular crystallography since then has been truly remarkable. What should we expect for the next decades?

In the realm of safe predictions we can expect the following:

  • (a) High-throughput macromolecular crystallography due to the developments outlined in Section 1.3.1[link], leading to the new field of `structural genomics'.

  • (b) Crystallography of very large complexes. While it is now clear that an atomic structure of a complex of 58 proteins and three RNA molecules, the ribosome, is around the corner, crystallographers will widen their horizons and start dreaming of structures like the nuclear pore complex, which has a molecular weight of over 100 000 000 Da.

  • (c) A steady flow of membrane protein structures. Whereas Max Perutz could only list five structures in his book of 1992, there are now over 40 PDB entries for membrane proteins. Most of them are transmembrane proteins: bacteriorhodopsin, photoreaction centres, light-harvesting complexes, cytochrome bc1 complexes, cytochrome c oxidases, photosystem I, porins, ion channels and bacterial toxins such as haemolysin and LukF. Others are monotopic membrane proteins such as squalene synthase and the cyclooxygenases. Clearly, membrane protein crystallography is gaining momentum at present and may open the door to atomic insight in neurotransmitter pharmacology in the next decade.

What if we dream beyond the obvious? One day, medicinal crystallography may contribute to:

  • (a) The design of submacromolecular agonists and antagonists of proteins and nucleic acids in a matter of a day by integrating rapid structure determinations, using only a few nanograms of protein, with the power of combinatorial and, in particular, computational chemistry.

  • (b) `Structural toxicology' based on `human structural genomics'. Once the hundreds of thousands of structures of human proteins and complexes with other proteins and nucleic acids have been determined, truly predictive toxicology may become possible. This will not only speed up the drug-development process, but may substantially reduce the suffering of animals in preclinical tests.

  • (c) The creation of completely new classes of drugs to treat addiction, organ regeneration, aging, memory enhancement etc.

One day, crystallography will have revealed the structure of hundreds of thousands of proteins and nucleic acids from human and pathogen, and their complexes with each other and with natural and designed low-molecular-weight ligands. This will form an extraordinarily precious database of knowledge for furthering the health of humans. Hence, in the course of the 21st century, crystallography is likely to become a major driving force for improving health care and disease prevention, and will find a well deserved place in future books describing progress in medicine, sometimes called `The Greatest Benefit to Mankind' (Porter, 1999[link]).

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