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| - | [[Image:2nml.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2nml| PDB=2nml | SCENE= }} | | {{STRUCTURE_2nml| PDB=2nml | SCENE= }} |
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| - | '''Crystal structure of HEF2/ERH at 1.55 A resolution'''
| + | ===Crystal structure of HEF2/ERH at 1.55 A resolution=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17444515}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17444515 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17444515}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pseudo beta barrel]] | | [[Category: Pseudo beta barrel]] |
| | [[Category: Transcription]] | | [[Category: Transcription]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:38:04 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:25:26 2008'' |
Revision as of 10:25, 28 July 2008
Template:STRUCTURE 2nml
Crystal structure of HEF2/ERH at 1.55 A resolution
Template:ABSTRACT PUBMED 17444515
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
Page seeded by OCA on Mon Jul 28 13:25:26 2008
