ATP binding domain 4 References

Bork, P & Koonin, E.V. (1994). ‘A P-Loop-Like Motif in a Widespread ATP Pyrophosphatase Domain: Implications for the Evolution of Sequence Motifs and Enzyme Activity.’Proteins: Structure, Function and Genetics 20:347-355.

Gough, J., Karplus, K., Hughey, R. and Chothia, C. (2001). ‘Assignment of Homology to Genome Sequences using a Library of Hidden Markov Models that Represent all Proteins of Known Structure.’ J. Mol. Biol., 313(4):903-919.

Horiike, T., Hamada, K., Kanaya, S. and Shinozawa, T. (2001). 'Origin of Eukaryotic Cell Nuclei by Symbiosis of Archaea in Bacteria is Revealed By Homology-hit Analysis.' Nature Cell Biology 3: 210-214. Katz, L.A.(1998). 'Changing Perspectives On The Origin of Eukaryotes.' Trends in Ecology and Evolution 1998, 13: 493-497.

Krissinel, E and Henrick, K. (2004). ‘Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions.’ Acta Cryst. D60:2256-2268.

Laskowski, R. A., N. M. Luscombe, et al. (1996). ‘Protein clefts in molecular recognition and function.’Protein Sci 5(12): 2438-52.

Lemke, C, T. and Howell, P.L. (2001). ‘The 1.6A Crystal Structure of E.coli Argininosuccinate Synthetase Suggests a Confomational Change during Catalysis.’ Structure 9:1153-1164.

Liang, J., H. Edelsbrunner, et al. (1998). ‘Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design.’Protein Sci 7(9): 1884-97.

Pal, D., Suhnel, J. and Weiss, M.S. (2002). ‘New principles of protein structure: nests, eggs - and what next?’ Angew. Chem. Int. Ed. 41:4663-4665.

Watson, J.D. and Milner-White, E.J. (2002). ‘A novel main-chain anion-binding site in proteins: the nest. A particular combination of phi,psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions.’ J. Mol. Biol. 315:171-82.

Watson, J.D. and Milner-White, E.J. (2002). ‘The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins.’ J. Mol. Biol. 315:183-191.

Abstract| Introductions| Methods|
Structural Analysis| Functional Analysis| Evolutionary Analysis|
Discussions| Conclusion | References

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