2nml
From Proteopedia
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| - | [[Image:2nml.jpg|left|200px]] | + | [[Image:2nml.jpg|left|200px]] |
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| - | '''Crystal structure of HEF2/ERH at 1.55 A resolution''' | + | {{Structure |
| + | |PDB= 2nml |SIZE=350|CAPTION= <scene name='initialview01'>2nml</scene>, resolution 1.550Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= ERH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of HEF2/ERH at 1.55 A resolution''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NML is a [ | + | 2NML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 2I4F. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NML OCA]. |
==Reference== | ==Reference== | ||
| - | A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks., Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ, Proteins. 2007 Aug 1;68(2):427-37. PMID:[http:// | + | A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks., Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ, Proteins. 2007 Aug 1;68(2):427-37. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17444515 17444515] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription]] | [[Category: transcription]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:48:15 2008'' |
Revision as of 15:48, 20 March 2008
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| , resolution 1.550Å | |||||||
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| Gene: | ERH (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HEF2/ERH at 1.55 A resolution
Overview
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 silico 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 alpha + beta fold, a four-strand antiparallel beta-sheet with three alpha-helixes on one side of the sheet. The beta-sheets from the two monomers together constitute a pseudo-beta-barrel, and form the center of the functional HEF2/ERH dimer, with a cavity channel at the dimer interface. Docking of this structure to the HEF2/ERH partner protein DCOH/PCD suggests that HEF2/ERH may regulate the oligomeric state of this protein. These data suggest that HEF2/ERH may be an important transcription regulator that also functions in the control of cell-cycle progression.
About this Structure
2NML is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2I4F. Full crystallographic information is available from OCA.
Reference
A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks., Jin T, Guo F, Serebriiskii IG, Howard A, Zhang YZ, Proteins. 2007 Aug 1;68(2):427-37. PMID:17444515
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