2kdi: Difference between revisions
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==Solution structure of a Ubiquitin/UIM fusion protein== | ==Solution structure of a Ubiquitin/UIM fusion protein== | ||
<StructureSection load='2kdi' size='340' side='right'caption='[[2kdi | <StructureSection load='2kdi' size='340' side='right'caption='[[2kdi]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2kdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2kdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDI FirstGlance]. <br> | ||
</td></tr> | </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=2kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdi OCA], [https://pdbe.org/2kdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdi RCSB], [https://www.ebi.ac.uk/pdbsum/2kdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdi ProSAT]</span></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=2kdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdi OCA], [https://pdbe.org/2kdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdi RCSB], [https://www.ebi.ac.uk/pdbsum/2kdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdi ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/UBI4P_YEAST UBI4P_YEAST] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: | [[Category: Garcia AE]] | ||
[[Category: | [[Category: Makhatadze GI]] | ||
[[Category: | [[Category: McCallum SA]] | ||
[[Category: | [[Category: Patel MM]] | ||
[[Category: | [[Category: Sgourakis NG]] | ||