4u4h
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of HSV-1 UL21 N-terminal Domain== | |
| + | <StructureSection load='4u4h' size='340' side='right'caption='[[4u4h]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4u4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U4H FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4u4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u4h OCA], [https://pdbe.org/4u4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u4h RCSB], [https://www.ebi.ac.uk/pdbsum/4u4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u4h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TEG4_HHV11 TEG4_HHV11] May participate in DNA packaging/capsid maturation events. Promotes efficient incorporation of tegument proteins UL46, UL49, and US3 into virions. May also play a role in capsid transport to the trans-Golgi network (TGN) (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | UL21 is a conserved protein in the tegument in alphaherpesviruses and has multiple important albeit poorly understood functions in viral replication and pathogenesis. To provide a roadmap for exploration of the multiple roles of UL21, we determined the crystal structure of its conserved N-terminal domain from Herpes Simplex virus Type 1 to 2.0-A resolution, which revealed a novel sail-like protein fold. Evolutionarily conserved surface patches highlight residues of potential importance for future targeting by mutagenesis. | ||
| - | + | The unusual fold of HSV-1 UL21, a multifunctional tegument protein.,Metrick CM, Chadha P, Heldwein EE J Virol. 2014 Dec 24. pii: JVI.03516-14. PMID:25540382<ref>PMID:25540382</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4u4h" style="background-color:#fffaf0;"></div> |
| - | [[Category: Heldwein | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human alphaherpesvirus 1 strain 17]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Heldwein EE]] | ||
| + | [[Category: Metrick CM]] | ||
Current revision
Crystal Structure of HSV-1 UL21 N-terminal Domain
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