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Protein Structure Prediction for the Male-Specific Region of the Human Y Chromosome
Krzysztof Ginalski, Leszek Rychlewski, David Baker, Nick V. Grishin and John Kuriyan
Proceedings of the National Academy of Sciences of the United States of America
Vol. 101, No. 8 (Feb. 24, 2004), pp. 2305-2310
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3371287
Page Count: 6
You can always find the topics here!Topics: Proteins, Zinc, Genes, Ubiquitins, Databases, Amino acids, Human Y chromosome, Sex determination, Modeling, Molecular structure
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The complete sequence of the male-specific region of the human Y chromosome (MSY) has been determined recently; however, detailed characterization for many of its encoded proteins still remains to be done. We applied state-of-the-art protein structure prediction methods to all 27 distinct MSY-encoded proteins to provide better understanding of their biological functions and their mechanisms of action at the molecular level. The results of such large-scale structure-functional annotation provide a comprehensive view of the MSY proteome, shedding light on MSY-related processes. We found that, in total, at least 60 domains are encoded by 27 distinct MSY genes, of which 42 (70%) were reliably mapped to currently known structures. The most challenging predictions include the unexpected but confident 3D structure assignments for three domains identified here encoded by the USP9Y, UTY, and BPY2 genes. The domains with unknown 3D structures that are not predictable with currently available theoretical methods are established as primary targets for crystallographic or NMR studies. The data presented here set up the basis for additional scientific discoveries in human biology of the Y chromosome, which plays a fundamental role in sex determination.
Proceedings of the National Academy of Sciences of the United States of America © 2004 National Academy of Sciences