1mv0

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[[Image:1mv0.jpg|left|200px]]
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{{Seed}}
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[[Image:1mv0.png|left|200px]]
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{{STRUCTURE_1mv0| PDB=1mv0 | SCENE= }}
{{STRUCTURE_1mv0| PDB=1mv0 | SCENE= }}
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'''NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC'''
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===NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC===
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==Overview==
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The N terminus of the c-Myc oncoprotein interacts with Bin1, a ubiquitously expressed nucleocytoplasmic protein with features of a tumor suppressor. The c-Myc/Bin1 interaction is dependent on the highly conserved Myc Box 1 (MB1) sequence of c-Myc. The c-Myc/Bin1 interaction has potential regulatory significance as c-Myc-mediated transformation and apoptosis can be modulated by the expression of Bin1. Multiple splicing of the Bin1 transcript results in ubiquitous, tissue-specific and tumor-specific populations of Bin1 proteins in vivo. We report on the structural features of the interaction between c-Myc and Bin1, and describe two mechanisms by which the binding of different Bin1 isoforms to c-Myc may be regulated in cells. Our findings identify a consensus class II SH3-binding motif in c-Myc and the C-terminal SH3 domain of Bin1 as the primary structure determinants of their interaction. We present biochemical and structural evidence that tumor-specific isoforms of Bin1 are precluded from interaction with c-Myc through an intramolecular polyproline-SH3 domain interaction that inhibits the Bin1 SH3 domain from binding to c-Myc. Furthermore, c-Myc/Bin1 interaction can be inhibited by phosphorylation of c-Myc at Ser62, a functionally important residue found within the c-Myc SH3-binding motif. Our data provide a structure-based model of the c-Myc/Bin1 interaction and suggest a mode of regulation that may be important for c-Myc function as a regulator of gene transcription.
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(as it appears on PubMed at http://www.pubmed.gov), where 15992821 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15992821}}
==About this Structure==
==About this Structure==
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1MV0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MV0 OCA].
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1MV0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MV0 OCA].
==Reference==
==Reference==
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[[Category: Pineda-Lucena, A.]]
[[Category: Pineda-Lucena, A.]]
[[Category: Tumor suppressor/oncoprotein]]
[[Category: Tumor suppressor/oncoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:45:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:28:09 2008''

Revision as of 13:28, 28 July 2008

Image:1mv0.png

Template:STRUCTURE 1mv0

NMR STRUCTURE OF THE TUMOR SUPPRESSOR BIN1: ALTERNATIVE SPLICING IN MELANOMA AND INTERACTION WITH C-MYC

Template:ABSTRACT PUBMED 15992821

About this Structure

1MV0 is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

Reference

A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants., Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, Muhandiram R, Lu Y, Seet BT, Katz S, Szyperski T, Penn LZ, Arrowsmith CH, J Mol Biol. 2005 Aug 5;351(1):182-94. PMID:15992821

Page seeded by OCA on Mon Jul 28 16:28:09 2008

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