Fadda, Elisa (2013) Conformational Determinants for the Recruitment of ERCC1 by XPA in the Nucleotide Excision Repair (NER) Pathway: Structure and Dynamics of the XPA Binding Motif. Biophysical Journal, 104 (11). pp. 2503-2511. ISSN 0006-3495

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Abstract

PA is an essential protein in the nucleotide excision repair (NER) pathway, in charge of recruiting the ERCC1- XPF endonuclease complex to the DNA damage site. The only currently available structural insight into the binding of XPA to ERCC1 derives from the solution NMR structure of a complex between the ERCC1 central fragment and a 14-residue peptide, corresponding to the highly conserved binding motif of the XPA N-terminus, XPA 67-80 . The extensive all-atom molecular- dynamics simulation study of the XPA 67-80 peptide both bound to the ERCC1 central fragment and free in solution presented here completes the profile of the structural determinants responsible for the ERCC1/XPA 67-80 complex stability. In addition to the wild-type, this study also looks at specific XPA 67-80 mutants in complex with the ERCC1 central domain and thus contributes to defining the conformational determinants for binding, as well as all of the essential structural elements necessary for the rational design of an XPA-based, ERCC1-specific inhibitor.

Item Type:	Article
Keywords:	ERCC1; XPA; Nucleotide Excision Repair; NER; XPA Binding Motif;
Academic Unit:	Faculty of Science and Engineering > Chemistry
Item ID:	4816
Identification Number:	https://doi.org/10.1016/j.bpj.2013.04.023
Depositing User:	Elisa Fadda
Date Deposited:	11 Mar 2014 17:26
Journal or Publication Title:	Biophysical Journal
Publisher:	Biophysical Society
Refereed:	Yes
URI:	Publisher
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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