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Protein structure modeling for structural genomics

Abstract

The shapes of most protein sequences will be modeled based on their similarity to experimentally determined protein structures. The current role, limitations, challenges and prospects for protein structure modeling (using information about genes and genomes) are discussed in the context of structural genomics.

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Figure 1: Distribution of the % sequence identity between the known protein structures and proteins of Mycobaterium genitalium, modeled as in ref. 13 in February, 2000.
Figure 2: Applications of comparative modeling.
Figure 3: Simulated effect of PDB growth on fold assignment and modeling coverage of the Mycoplasma genitalium proteins.

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Acknowledgements

We are most grateful to S.K. Burley, T. Gaasterland, J. Kuriyan, J. Bonanno, M. Chance, S. Almo, L. Shapiro, C. Lima and other members of the New York Structural Genomics Research Consortium for many discussions about structural genomics. We also thank J.P. Overington for comments on the manuscript. R.S. is a Howard Hughes Medical Institute predoctoral fellow. A.S. is an Alfred P. Sloan Research Fellow and an Irma T. Hirschl Trust Career Scientist. Support from The Merck Genome Research Institute, Mathers Foundation, the NSF, and the NIH is also acknowledged.

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Correspondence to Andrej Šali.

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Sánchez, R., Pieper, U., Melo, F. et al. Protein structure modeling for structural genomics. Nat Struct Mol Biol 7 (Suppl 11), 986–990 (2000). https://doi.org/10.1038/80776

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