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Jin TC, Guo F, Serebriiskii IG, Howard A, Zhang YZ
A 1.55 a resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks
Proteins-Structure Function and Bioinformatics (2007) 68:427-437.
Abstract
Functional complementation screens can identify known or novel proteins with important intracellular activities. We have isolated human enhancer of filamentation 2 (HEF2) in a screen to find human genes that promote pseudohyphal growth in budding yeast. HEF2 is identical to enhancer of rudimentary homolog (ERH), a highly conserved protein of 104 amino acids. In sitico protein-interaction mapping implies that HEF2/ERH interacts with transcription factors, cell-cycle regulators, and other proteins shown to enhance filamentous growth in S. cerevisiae, suggesting a context for studies of HEF2/ERH function. To provide a mechanistic basis to study of HEF2/ERH, we have determined the crystal structure of HEF2/ERH at 1.55 A. The crystal asymmetric unit contains a HEF2/ERH monomer. The two monomers of the physiological dimer are related by the y, x, -z crystal symmetric operation. The HEF2/ERH structure is characterized by a novel a + 0 fold, a four-strand antiparallel P-sheet wit!
Note
Publication Date: 2007-08-01.
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