2nml

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{{Seed}}
 
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[[Image:2nml.png|left|200px]]
 
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==Crystal structure of HEF2/ERH at 1.55 A resolution==
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The line below this paragraph, containing "STRUCTURE_2nml", creates the "Structure Box" on the page.
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<StructureSection load='2nml' size='340' side='right'caption='[[2nml]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2nml]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2i4f 2i4f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NML FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2nml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nml OCA], [https://pdbe.org/2nml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nml RCSB], [https://www.ebi.ac.uk/pdbsum/2nml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nml ProSAT]</span></td></tr>
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{{STRUCTURE_2nml| PDB=2nml | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ERH_HUMAN ERH_HUMAN] May have a role in the cell cycle.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/2nml_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2nml ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of HEF2/ERH at 1.55 A resolution===
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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<ref>PMID:17444515</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_17444515}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2nml" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17444515 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17444515}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2NML is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2i4f 2i4f]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NML OCA].
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==Reference==
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<ref group="xtra">PMID:17444515</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Guo, F.]]
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[[Category: Large Structures]]
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[[Category: Howard, A J.]]
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[[Category: Guo F]]
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[[Category: Jin, T C.]]
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[[Category: Howard AJ]]
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[[Category: Serebriiskii, I G.]]
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[[Category: Jin TC]]
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[[Category: Zhang, Y Z.]]
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[[Category: Serebriiskii IG]]
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[[Category: Cell cycle]]
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[[Category: Zhang YZ]]
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[[Category: Hef2/erh fold]]
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[[Category: Interaction network]]
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[[Category: Pseudo beta barrel]]
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[[Category: Transcription]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:45:16 2009''
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Current revision

Crystal structure of HEF2/ERH at 1.55 A resolution

PDB ID 2nml

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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