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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V.

Mlc1p is a calmodulin-like protein from the budding yeast Saccharomyces cerevisiae, where it has been identified as a subunit of a class V myosin, Myo2p, and a binding partner of an IQGAP-like protein, Iqg1p. Through its interactions with these two proteins, Mlc1p plays a role in polarized growth and cytokinesis. Mlc1p has been crystallized in complexes with four different IQ target motifs from the neck region of Myo2p: IQ2, IQ3, IQ4 and IQ2-IQ3 (referred to as IQ2,3). Electron-density maps for two of the complexes (Mlc1p-IQ4 and Mlc1p-IQ2,3) were obtained from multiple anomalous dispersion (MAD) experiments based on selenomethionine derivatives. The other two structures (Mlc1p-IQ2 and Mlc1p-IQ3) were determined by molecular replacement using the partially refined structure of Mlc1p-IQ2,3 as a search model.[1]

References

  1. Crystallization, X-ray characterization and selenomethionine phasing of Mlc1p bound to IQ motifs from myosin V. Terrak, M., Otterbein, L.R., Wu, G., Palecanda, L.A., Lu, R.C., Dominguez, R. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
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