PMID- 24389026
OWN - NLM
STAT- MEDLINE
DCOM- 20141022
LR  - 20240210
IS  - 1878-4186 (Electronic)
IS  - 0969-2126 (Print)
IS  - 0969-2126 (Linking)
VI  - 22
IP  - 2
DP  - 2014 Feb 4
TI  - Structure of the human FANCL RING-Ube2T complex reveals determinants of cognate 
      E3-E2 selection.
PG  - 337-44
LID - S0969-2126(13)00466-8 [pii]
LID - 10.1016/j.str.2013.12.004 [doi]
AB  - The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase 
      is essential for ubiquitin modification of a substrate. Moreover, the pairing 
      dictates both the substrate choice and the modification type. The molecular 
      details of generic E3-E2 interactions are well established. Nevertheless, the 
      determinants of selective, specific E3-E2 recognition are not understood. There 
      are  approximately 40 E2s and  approximately 600 E3s giving rise to a possible  approximately 24,000 E3-E2 pairs. Using the 
      Fanconi Anemia pathway exclusive E3-E2 pair, FANCL-Ube2T, we report the atomic 
      structure of the FANCL RING-Ube2T complex, revealing a specific and extensive 
      network of additional electrostatic and hydrophobic interactions. Furthermore, we 
      show that these specific interactions are required for selection of Ube2T over 
      other E2s by FANCL.
CI  - Copyright (c) 2014 The Authors. Published by Elsevier Inc. All rights reserved.
FAU - Hodson, Charlotte
AU  - Hodson C
AD  - Protein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of 
      the London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, 
      London WC2A 3LY, UK.
FAU - Purkiss, Andrew
AU  - Purkiss A
AD  - Protein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of 
      the London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, 
      London WC2A 3LY, UK.
FAU - Miles, Jennifer Anne
AU  - Miles JA
AD  - Protein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of 
      the London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, 
      London WC2A 3LY, UK.
FAU - Walden, Helen
AU  - Walden H
AD  - Protein Structure and Function Laboratory, Lincoln's Inn Fields Laboratories of 
      the London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, 
      London WC2A 3LY, UK; MRC-Protein Phosphorylation and Ubiquitylation Unit, College 
      of Life Sciences, Dow Street, Dundee DD1 5EH, UK. Electronic address: 
      h.walden@dundee.ac.uk.
LA  - eng
GR  - 17739/CRUK_/Cancer Research UK/United Kingdom
GR  - MC_UU_12016/12/MRC_/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140102
PL  - United States
TA  - Structure
JT  - Structure (London, England : 1993)
JID - 101087697
RN  - 0 (Ubiquitin)
RN  - EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
RN  - EC 2.3.2.27 (FANCL protein, human)
RN  - EC 2.3.2.27 (Fanconi Anemia Complementation Group L Protein)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - DNA Repair
MH  - Fanconi Anemia Complementation Group L Protein/*chemistry
MH  - Humans
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Protein Conformation
MH  - Sequence Homology, Amino Acid
MH  - Ubiquitin/chemistry
MH  - Ubiquitin-Conjugating Enzymes/metabolism
MH  - Ubiquitin-Protein Ligases/chemistry
MH  - Xenopus laevis
PMC - PMC3979106
EDAT- 2014/01/07 06:00
MHDA- 2014/10/23 06:00
PMCR- 2014/02/04
CRDT- 2014/01/07 06:00
PHST- 2013/08/02 00:00 [received]
PHST- 2013/11/21 00:00 [revised]
PHST- 2013/12/02 00:00 [accepted]
PHST- 2014/01/07 06:00 [entrez]
PHST- 2014/01/07 06:00 [pubmed]
PHST- 2014/10/23 06:00 [medline]
PHST- 2014/02/04 00:00 [pmc-release]
AID - S0969-2126(13)00466-8 [pii]
AID - 10.1016/j.str.2013.12.004 [doi]
PST - ppublish
SO  - Structure. 2014 Feb 4;22(2):337-44. doi: 10.1016/j.str.2013.12.004. Epub 2014 Jan 
      2.