File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Structure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins.

TitleStructure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins.
Authors
Issue Date2014
PublisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/
Citation
The FEBS Journal, 2014, v. 281 n. 15, p. 3382-96 How to Cite?
AbstractReplication protein A subunit RPA32 contains a C-terminal domain that interacts with a variety of DNA damage response proteins including SMARCAL1, Tipin, UNG2 and XPA. We have solved the high-resolution crystal structure of RPA32 C-terminal domain (RPA32C) in complex with a 26-amino-acid peptide derived from the N-terminus of SMARCAL1 (SMARCAL1N). The RPA32C-SMARCAL1N structure reveals a 1 : 1 binding stoichiometry and displays a well-ordered binding interface. SMARCAL1N adopts a long α-helical conformation with the highly conserved 11 residues aligned on one face of the α-helix showing extensive interactions with the RPA32C domain. Extensive mutagenesis experiments were performed to corroborate the interactions observed in crystal structure. Moreover, the α1/α2 loop of the RPA32C domain undergoes a conformational rearrangement upon SMARCAL1N binding. NMR study has further confirmed that the RPA32C-SMARCAL1N interaction induces conformational changes in RPA32C. Isothermal titration calorimetry studies have also demonstrated that the conserved α-helical motif defined in the current study is required for sufficient binding of RPA32C. Taken together, our study has provided convincing structural information that redefines the common recognition pattern shared by RPA32C interacting proteins.
Persistent Identifierhttp://hdl.handle.net/10722/202515
ISSN
2015 Impact Factor: 4.237
2015 SCImago Journal Rankings: 2.141
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorXIE, S-
dc.contributor.authorLU, Y-
dc.contributor.authorJakoncic, J-
dc.contributor.authorSun, H-
dc.contributor.authorXIA, J-
dc.contributor.authorQian, C-
dc.date.accessioned2014-09-19T08:25:11Z-
dc.date.available2014-09-19T08:25:11Z-
dc.date.issued2014-
dc.identifier.citationThe FEBS Journal, 2014, v. 281 n. 15, p. 3382-96-
dc.identifier.issn1742-464X-
dc.identifier.urihttp://hdl.handle.net/10722/202515-
dc.description.abstractReplication protein A subunit RPA32 contains a C-terminal domain that interacts with a variety of DNA damage response proteins including SMARCAL1, Tipin, UNG2 and XPA. We have solved the high-resolution crystal structure of RPA32 C-terminal domain (RPA32C) in complex with a 26-amino-acid peptide derived from the N-terminus of SMARCAL1 (SMARCAL1N). The RPA32C-SMARCAL1N structure reveals a 1 : 1 binding stoichiometry and displays a well-ordered binding interface. SMARCAL1N adopts a long α-helical conformation with the highly conserved 11 residues aligned on one face of the α-helix showing extensive interactions with the RPA32C domain. Extensive mutagenesis experiments were performed to corroborate the interactions observed in crystal structure. Moreover, the α1/α2 loop of the RPA32C domain undergoes a conformational rearrangement upon SMARCAL1N binding. NMR study has further confirmed that the RPA32C-SMARCAL1N interaction induces conformational changes in RPA32C. Isothermal titration calorimetry studies have also demonstrated that the conserved α-helical motif defined in the current study is required for sufficient binding of RPA32C. Taken together, our study has provided convincing structural information that redefines the common recognition pattern shared by RPA32C interacting proteins.-
dc.languageeng-
dc.publisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/-
dc.relation.ispartofThe FEBS Journal-
dc.rightsPreprint This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article]. Authors are not required to remove preprints posted prior to acceptance of the submitted version. Postprint This is the accepted version of the following article: [full citation], which has been published in final form at [Link to final article].-
dc.titleStructure of RPA32 bound to the N-terminus of SMARCAL1 redefines the binding interface between RPA32 and its interacting proteins.-
dc.typeArticle-
dc.identifier.emailSun, H: hsun@hku.hk-
dc.identifier.emailQian, C: cmqian@hku.hk-
dc.identifier.authoritySun, H=rp00777-
dc.identifier.authorityQian, C=rp01371-
dc.identifier.doi10.1111/febs.12867-
dc.identifier.pmid24910198-
dc.identifier.scopuseid_2-s2.0-84905159139-
dc.identifier.hkuros237284-
dc.identifier.volume281-
dc.identifier.issue15-
dc.identifier.spage3382-
dc.identifier.epage96-
dc.identifier.isiWOS:000340355300006-
dc.publisher.placeUnited Kingdom-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats