1nj3

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(New page: 200px<br /><applet load="1nj3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nj3" /> '''Structure and Ubiquitin Interactions of the ...)
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[[Image:1nj3.gif|left|200px]]<br /><applet load="1nj3" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4'''<br />
'''Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4'''<br />
==Overview==
==Overview==
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Ubiquitylated proteins are directed into a large number of different, cellular pathways through interactions with effector proteins that contain, conserved ubiquitin binding motifs. Here, we report the solution structure, and ubiquitin binding properties of one such motif, the Npl4 zinc finger, or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module, composed of four antiparallel beta-strands linked by three ordered loops., A single zinc ion is coordinated by four conserved cysteines from the, first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds, specifically, but weakly, to free ubiquitin using a conserved 13TF14, dipeptide to interact with the "Ile-44" surface of ubiquitin. Our studies, reveal the structure of this versatile class of protein binding domains, and provide a means for identifying the subset of NZF domains likely to, bind ubiquitin.
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Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteines from the first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds specifically, but weakly, to free ubiquitin using a conserved 13TF14 dipeptide to interact with the "Ile-44" surface of ubiquitin. Our studies reveal the structure of this versatile class of protein binding domains and provide a means for identifying the subset of NZF domains likely to bind ubiquitin.
==About this Structure==
==About this Structure==
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1NJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NJ3 OCA].
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1NJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NJ3 OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Alam, S.L.]]
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[[Category: Alam, S L.]]
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[[Category: Davis, D.R.]]
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[[Category: Davis, D R.]]
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[[Category: Meyer, H.H.]]
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[[Category: Meyer, H H.]]
[[Category: Payne, M.]]
[[Category: Payne, M.]]
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[[Category: Stemmler, T.L.]]
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[[Category: Stemmler, T L.]]
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[[Category: Sundquist, W.I.]]
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[[Category: Sundquist, W I.]]
[[Category: Wang, B.]]
[[Category: Wang, B.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:18:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:37 2008''

Revision as of 12:06, 21 February 2008


1nj3

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Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4

Overview

Ubiquitylated proteins are directed into a large number of different cellular pathways through interactions with effector proteins that contain conserved ubiquitin binding motifs. Here, we report the solution structure and ubiquitin binding properties of one such motif, the Npl4 zinc finger or RanBP2/Nup358 zinc finger (NZF) domain. Npl4 NZF forms a compact module composed of four antiparallel beta-strands linked by three ordered loops. A single zinc ion is coordinated by four conserved cysteines from the first and third loops, which form two rubredoxin knuckles. Npl4 NZF binds specifically, but weakly, to free ubiquitin using a conserved 13TF14 dipeptide to interact with the "Ile-44" surface of ubiquitin. Our studies reveal the structure of this versatile class of protein binding domains and provide a means for identifying the subset of NZF domains likely to bind ubiquitin.

About this Structure

1NJ3 is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4., Wang B, Alam SL, Meyer HH, Payne M, Stemmler TL, Davis DR, Sundquist WI, J Biol Chem. 2003 May 30;278(22):20225-34. Epub 2003 Mar 18. PMID:12644454

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