2mbo

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m (Protected "2mbo" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_2mbo| PDB=2mbo | SCENE= }}
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===K11-linked Diubiquitin average solution structure at pH 6.8, 0 mM NaCl===
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{{ABSTRACT_PUBMED_23823328}}
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The entry 2mbo is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] 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, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. 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.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
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Authors: Castaneda, C.A., Fushman, D.
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==About this Structure==
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[[2mbo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBO OCA].
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Description: K11-linked Diubiquitin average solution structure at pH 6.8, 0 mM NaCl
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==Reference==
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<ref group="xtra">PMID:023823328</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Castaneda, C A.]]
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[[Category: Fushman, D.]]
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[[Category: Diubiquitin]]
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[[Category: K11]]
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[[Category: Signaling protein]]

Revision as of 10:50, 4 September 2013

Template:STRUCTURE 2mbo

Contents

K11-linked Diubiquitin average solution structure at pH 6.8, 0 mM NaCl

Template:ABSTRACT PUBMED 23823328

Function

[UBC_HUMAN] 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, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. 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.[1] [2]

About this Structure

2mbo is a 2 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

  • Castaneda CA, Kashyap TR, Nakasone MA, Krueger S, Fushman D. Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains. Structure. 2013 Jul 2;21(7):1168-81. doi: 10.1016/j.str.2013.04.029. PMID:23823328 doi:10.1016/j.str.2013.04.029
  1. Huang F, Kirkpatrick D, Jiang X, Gygi S, Sorkin A. Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain. Mol Cell. 2006 Mar 17;21(6):737-48. PMID:16543144 doi:S1097-2765(06)00120-1
  2. Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans. 2009 Oct;37(Pt 5):937-53. doi: 10.1042/BST0370937. PMID:19754430 doi:10.1042/BST0370937

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