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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004160naa a2200445 4500
001oai:DiVA.org:liu-82076
003SwePub
008120928s2012 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-820762 URI
0247 a https://doi.org/10.1093/nar/gks2632 DOI
040 a (SwePub)liu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Andrésen, Ceciliau Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan4 aut0 (Swepub:liu)cecan53
2451 0a Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding
264 c 2012-03-28
264 1b Oxford University Press (OUP): Policy C / Oxford University Press,c 2012
338 a electronic2 rdacarrier
500 a Funding Agencies|VINNOVA||CIHR||Swedish Research Council||Swedish Cancer Foundation||Swedish Child Cancer Foundation||Canadian Cancer Society||Ontario Research Fund|GL2-01-030|NIH Protein Structure Initiative grant|U54 GM094597|Canada Research Chairs Program||Swedish NMR Centre||Knut and Alice Wallenberg Foundation||Linkoping University||
520 a The crucial role of Myc as an oncoprotein and as a key regulator of cell growth makes it essential to understand the molecular basis of Myc function. The N-terminal region of c-Myc coordinates a wealth of protein interactions involved in transformation, differentiation and apoptosis. We have characterized in detail the intrinsically disordered properties of Myc-1-88, where hierarchical phosphorylation of S62 and T58 regulates activation and destruction of the Myc protein. By nuclear magnetic resonance (NMR) chemical shift analysis, relaxation measurements and NOE analysis, we show that although Myc occupies a very heterogeneous conformational space, we find transiently structured regions in residues 22-33 and in the Myc homology box I (MBI; residues 45-65); both these regions are conserved in other members of the Myc family. Binding of Bin1 to Myc-1-88 as assayed by NMR and surface plasmon resonance (SPR) revealed primary binding to the S62 region in a dynamically disordered and multivalent complex, accompanied by population shifts leading to altered intramolecular conformational dynamics. These findings expand the increasingly recognized concept of intrinsically disordered regions mediating transient interactions to Myc, a key transcriptional regulator of major medical importance, and have important implications for further understanding its multifaceted role in gene regulation.
653 a TECHNOLOGY
653 a TEKNIKVETENSKAP
7001 a Helander, Sarau Linköpings universitet,Kemi,Tekniska fakulteten4 aut0 (Swepub:liu)sarhe49
7001 a Lemak, Alexanderu University of Toronto, Canada4 aut
7001 a Fares, Christopheu University of Toronto, Canada4 aut
7001 a Csizmok, Veronikau Hospital for Sick Children, Canada4 aut
7001 a Carlsson, Jonasu Linköpings universitet,Bioinformatik,Tekniska högskolan4 aut0 (Swepub:liu)jonca19
7001 a Penn, Linda Zu University of Toronto, Canada4 aut
7001 a Forman-Kay, Julie Du Hospital Sick Children, Canada University of Toronto, Canada4 aut
7001 a Arrowsmith, Cheryl Hu University of Toronto, Canada4 aut
7001 a Lundström, Patriku Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan4 aut0 (Swepub:liu)patlu71
7001 a Sunnerhagen, Mariau Linköpings universitet,Molekylär Bioteknik,Tekniska högskolan4 aut0 (Swepub:liu)marsu05
7102 a Linköpings universitetb Molekylär Bioteknik4 org
7730 t Nucleic Acids Researchd : Oxford University Press (OUP): Policy C / Oxford University Pressg 40:13, s. 6353-6366q 40:13<6353-6366x 0305-1048x 1362-4962
8564 u https://liu.diva-portal.org/smash/get/diva2:557695/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 u https://academic.oup.com/nar/article-pdf/40/13/6353/16964284/gks263.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-82076
8564 8u https://doi.org/10.1093/nar/gks263

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