2jyd

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(New page: 200px<br /><applet load="2jyd" size="350" color="white" frame="true" align="right" spinBox="true" caption="2jyd" /> '''Structure of the fifth zinc finger of Myelin...)
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==Overview==
==Overview==
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Zinc binding domains, or zinc fingers (ZnFs), form one of the most, numerous and most diverse superclasses of protein structural motifs in, eukaryotes. While our understanding of the functions of several classes of, these domains is relatively well developed, we know much less about the, molecular mechanisms of action of many others. Myelin transcription factor, 1 (MyT1) type ZnFs are found in organisms as diverse as nematodes and, mammals and are found in a range of sequence contexts. MyT1, one of the, early transcription factors expressed in the developing central nervous, system, contains seven MyT1 ZnFs that are very highly conserved both, within the protein and between species. We have used a range of, biophysical techniques, including NMR spectroscopy and data-driven, macromolecular docking, to investigate the structural basis for the, interaction between MyT1 ZnFs and DNA. Our data indicate that MyT1 ZnFs, recognize the major groove of DNA in a way that appears to differ from, other known zinc-binding domains.
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Zinc binding domains, or zinc fingers (ZnFs), form one of the most numerous and most diverse superclasses of protein structural motifs in eukaryotes. Although our understanding of the functions of several classes of these domains is relatively well developed, we know much less about the molecular mechanisms of action of many others. Myelin transcription factor 1 (MyT1) type ZnFs are found in organisms as diverse as nematodes and mammals and are found in a range of sequence contexts. MyT1, one of the early transcription factors expressed in the developing central nervous system, contains seven MyT1 ZnFs that are very highly conserved both within the protein and between species. We have used a range of biophysical techniques, including NMR spectroscopy and data-driven macromolecular docking, to investigate the structural basis for the interaction between MyT1 ZnFs and DNA. Our data indicate that MyT1 ZnFs recognize the major groove of DNA in a way that appears to differ from other known zinc binding domains.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Structural and biophysical analysis of the DNA-binding properties of myelin transcription factor 1., Gamsjaeger R, Swanton MK, Kobus FJ, Lehtomaki E, Lowry JA, Kwan AH, Matthews JM, Mackay JP, J Biol Chem. 2007 Dec 11;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073212 18073212]
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Structural and biophysical analysis of the DNA binding properties of myelin transcription factor 1., Gamsjaeger R, Swanton MK, Kobus FJ, Lehtomaki E, Lowry JA, Kwan AH, Matthews JM, Mackay JP, J Biol Chem. 2008 Feb 22;283(8):5158-67. Epub 2007 Dec 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18073212 18073212]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gamsjaeger, R.]]
[[Category: Gamsjaeger, R.]]
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[[Category: Kobus, F.J.]]
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[[Category: Kobus, F J.]]
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[[Category: Kwan, A.H.]]
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[[Category: Kwan, A H.]]
[[Category: Lehtomaki, E.]]
[[Category: Lehtomaki, E.]]
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[[Category: Lowry, J.A.]]
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[[Category: Lowry, J A.]]
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[[Category: Mackay, J.P.]]
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[[Category: Mackay, J P.]]
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[[Category: Matthews, J.M.]]
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[[Category: Matthews, J M.]]
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[[Category: Swanton, M.K.]]
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[[Category: Swanton, M K.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: alternative splicing]]
[[Category: alternative splicing]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:05:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:31 2008''

Revision as of 16:06, 21 February 2008


2jyd

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Structure of the fifth zinc finger of Myelin Transcription Factor 1

Overview

Zinc binding domains, or zinc fingers (ZnFs), form one of the most numerous and most diverse superclasses of protein structural motifs in eukaryotes. Although our understanding of the functions of several classes of these domains is relatively well developed, we know much less about the molecular mechanisms of action of many others. Myelin transcription factor 1 (MyT1) type ZnFs are found in organisms as diverse as nematodes and mammals and are found in a range of sequence contexts. MyT1, one of the early transcription factors expressed in the developing central nervous system, contains seven MyT1 ZnFs that are very highly conserved both within the protein and between species. We have used a range of biophysical techniques, including NMR spectroscopy and data-driven macromolecular docking, to investigate the structural basis for the interaction between MyT1 ZnFs and DNA. Our data indicate that MyT1 ZnFs recognize the major groove of DNA in a way that appears to differ from other known zinc binding domains.

About this Structure

2JYD is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural and biophysical analysis of the DNA binding properties of myelin transcription factor 1., Gamsjaeger R, Swanton MK, Kobus FJ, Lehtomaki E, Lowry JA, Kwan AH, Matthews JM, Mackay JP, J Biol Chem. 2008 Feb 22;283(8):5158-67. Epub 2007 Dec 11. PMID:18073212

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