1p0r: Difference between revisions
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<StructureSection load='1p0r' size='340' side='right'caption='[[1p0r]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1p0r' size='340' side='right'caption='[[1p0r]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1p0r]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1p0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P0R FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1p0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p0r OCA], [https://pdbe.org/1p0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p0r RCSB], [https://www.ebi.ac.uk/pdbsum/1p0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p0r ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 12:23, 8 September 2021
Solution Structure of UBL5 a human Ubiquitin-Like ProteinSolution Structure of UBL5 a human Ubiquitin-Like Protein
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedUBL5 is a widely expressed human protein that is strongly conserved across phylogeny. Orthologs of UBL5 occur in every eukaryotic genome characterized to date. The yeast ortholog of UBL5, HUB1, was reported to be a ubiquitin-like protein modifier important for modulation of protein function. However, unlike ubiquitin and all other ubiquitin-like modifiers, UBL5 and its yeast ortholog HUB1 both contain a C-terminal di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other ubiquitin-like modifiers. Here we describe the three-dimensional structure of UBL5 determined by NMR. The overall structure of the protein was found to be very similar to ubiquitin despite the low approximately 25% residue similarity. The signature C-terminal di-tyrosine residues in UBL5 are involved in the final beta sheet of the protein. This is very different to the di-glycine motif found in ubiquitin, which extends beyond the final beta sheet. In addition, we have confirmed an earlier report of an interaction between UBL5 and the cyclin-like kinase, CLK4, which we have determined is specific and does not extend to other cyclin-like kinase family members. Structural analysis of UBL5, a novel ubiquitin-like modifier.,McNally T, Huang Q, Janis RS, Liu Z, Olejniczak ET, Reilly RM Protein Sci. 2003 Jul;12(7):1562-6. PMID:12824502[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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