HUGO ID Detailed Result 3435

HUGO ID 3435
Symbol ERCC3
Name excision repair cross-complementing rodent repair deficiency, complementation group 3 (xeroderma pigmentosum group B complementing)
#Occurrence 63
#Paper 1

 

PMID Match String Actual String Score Flanking text Edited by Edit
17174478XPBXPB2.4Fig 7 XPB conserved motifs and structural architecture 
17174478XPBXPB2.4a Schematic alignment between Af XPB Af and human XPB Hs 
17174478XPBXPB2.4a Schematic alignment between Af XPB Af and human XPB Hs 
17174478XPBXPB2.4Fig 8 Proposed structure-based mechanism whereby damage verification by XPB promotes unwinding of damaged dsDNA for NER 
17174478XPBXPB2.4a Schematic model shows how XPB DRD depicted in blue HD1 cyan RED motif red HD2 
17174478XPBXPB2.4Af XPB Archaeoglobus fulgidus XPB AH auto-inhibitory helix ATLD ataxiatelangiectasia-like disorder BER 
17174478XPBXPB2.4Af XPB Archaeoglobus fulgidus XPB AH auto-inhibitory helix ATLD ataxiatelangiectasia-like disorder BER base excision repair 
17174478XPBXPB2.4NER and the XPB helicase 
17174478XPBXPB2.4gene that is associated with all three disorders is the XPB helicase ( Weeda et al. 1997 which is part of 
17174478TFIIHTFIIH2.7al. 1997 which is part of the general transcription factor TFIIH complex ( Schaeffer et al. 1993 
17174478XPBXPB2.4The XPB ATPase and helicase activities are essential for promoter DNA melting 
17174478XPBXPB2.4In addition to these transcriptional functions XPB also plays a role in NER 
17174478XPBXPB2.4Recent developments in structural and biochemical characterization of XPB helicase have begun to address some of the key questions 
17174478XPBXPB2.4of the key questions on the underlying mechanisms of how XPB and TFIIH function in both transcription and NER ( Coin 
17174478TFIIHTFIIH2.7key questions on the underlying mechanisms of how XPB and TFIIH function in both transcription and NER ( Coin et al. 
17174478XPBXPB2.4studies have been conducted on a homolog of the human XPB the archea Archaeoglobus fulgidus XPB ( Af XPB ( Fan 
17174478XPBXPB2.4a homolog of the human XPB the archea Archaeoglobus fulgidus XPB ( Af XPB ( Fan et al. 2006a 
17174478XPBXPB2.4the human XPB the archea Archaeoglobus fulgidus XPB ( Af XPB ( Fan et al. 2006a 
17174478XPBXPB2.4Af XPB shares 42% amino acid sequence similarity with the central region 
17174478XPBXPB2.4amino acid sequence similarity with the central region of human XPB suggesting that the core XPB structure is conserved 
17174478XPBXPB2.4the central region of human XPB suggesting that the core XPB structure is conserved 
17174478XPBXPB2.4As indicated by sequence comparison the Af XPB structure contains two RecA-like helicase domains (HD1 HD1 and HD2 
17174478XPBXPB2.4However several other functional regions in XPB were discovered that were not predicted either through sequence analysis 
17174478XPBXPB2.4This domain in Af XPB has been demonstrated to interact with some types of damaged 
17174478XPBXPB2.4XPB DRD differs from the MutS domain by lacking a critical 
17174478XPBXPB2.4Instead Af XPB DRD likely recognizes distortions in the DNA typically caused by 
17174478XPBXPB2.4to initiation of DNA unwinding during NER steps by XPB/TFIIH XPB TFIIH 
17174478TFIIHTFIIH2.7initiation of DNA unwinding during NER steps by XPB/TFIIH XPB TFIIH 
17174478XPBXPB-family2.4Also present is a highly conserved XPB-family specific RED amino acid motif located in domain HD1 ( 
17174478XPBXPB2.4Mutational analysis suggests that this XPB RED motif has a critical role in DNA unwinding function 
17174478XPBXPB2.4NER and the XPB helicase 
17174478XPBXPB2.4Af XPB seems to follow this general trend 
17174478XPBXPB2.4helicase domains HD1 and HD2 observed in the full-length Af XPB is different than the _amp_#x0201c closed_amp_#x0201d conformation observed in crystal 
17174478XPBXPB2.4also lead to a proposed mechanism for the involvement of XPB in the unwinding of duplex DNA at sites of DNA 
17174478XPBXPB2.4When XPB is recruited to DNA the DRD domain is proposed to 
17174478XPBXPB2.4helicase domain HD2 via a rotation of ~170_amp_#x000b0 and allows XPB to wrap around the DNA 
17174478XPBXPB2.4such a conformational change may result from interaction of the XPB C-terminus (including including ThM and HD2 domains with 3'-overhanging DNA 
17174478XPBXPB2.4_amp_#x0201c wedge_amp_#x0201d to unzip the DNA when ATP hydrolysis drives XPB to move along the duplex DNA during NER 
17174478XPBXPB2.4However it is noticed that DNA melting by XPB during transcription initiation is possibly mediated through an unconventional helicase 
17174478XPBXPB2.4unconventional helicase mechanism ( Kim et al. 2000 in which XPB functions as a molecular _amp_#x0201c wrench_amp_#x0201d rotating downstream DNA relative 
17174478XPBXPB2.4Therefore the conformation observed in the Af XPB structure may represent a _amp_#x0201c transcriptional mode_amp_#x0201d of XPB tuned 
17174478XPBXPB2.4Af XPB structure may represent a _amp_#x0201c transcriptional mode_amp_#x0201d of XPB tuned for this action whereas the domain reorientation described above 
17174478XPBXPB2.4If these mechanisms are true the conformation of XPB will decide whether TFIIH functions as a transcription factor or 
17174478TFIIHTFIIH2.7mechanisms are true the conformation of XPB will decide whether TFIIH functions as a transcription factor or a DNA repair factor 
17174478XPBXPB2.4In other words XPB acts as a master key helping TFIIH switch pathway selection 
17174478TFIIHTFIIH2.7In other words XPB acts as a master key helping TFIIH switch pathway selection for transcription or DNA repair whenever it 
17174478XPBXPB2.4NER and the XPB helicase 
17174478XPBXPB2.4Defining the Af XPB structural biochemistry has uncovered some unexpected structural motifs and functions 
17174478XPBXPB2.4biochemistry has uncovered some unexpected structural motifs and functions for XPB 
17174478XPBXPB2.4However Af XPB only correlates to the central region of human XPB 
17174478XPBXPB2.4Af XPB only correlates to the central region of human XPB 
17174478XPBXPB2.4exclusively occur in the N- and C-terminal extensions of human XPB suggesting that mutation to the conserved XPB central region is 
17174478XPBXPB2.4extensions of human XPB suggesting that mutation to the conserved XPB central region is lethal 
17174478XPBXPB2.4Af XPB reflects the basic structure and function of XPB helicases 
17174478XPBXPB2.4Af XPB reflects the basic structure and function of XPB helicases 
17174478XPBXPB2.4However the extensions to the human XPB are likely to contribute to a greater level of complexity 
17174478XPBXPB2.4Phosphorylation of residue S751 at the C-terminal extension of human XPB was reported to regulate TFIIH activity in NER reactions ( 
17174478TFIIHTFIIH2.7the C-terminal extension of human XPB was reported to regulate TFIIH activity in NER reactions ( Coin et al. 2004 
17174478XPBXPB2.4The physical and functional interactions between XPB and other proteins within and outside of the TFIIH complex 
17174478TFIIHTFIIH2.7between XPB and other proteins within and outside of the TFIIH complex have been investigated recently ( Jawhari et al. 2002 
17174478TFIIHTFIIH2.7occur in the extensions and have profound effects on the TFIIH activities in transcription or DNA repair 
17174478XPBXPB2.4that future studies will similarly uncover new functions for human XPB 
17174478TFIIHTFIIH2.7features highlighted above will fit into the ring-structure of human TFIIH complex ( Chang and Kornberg 2000 Schultz et al. 2000