1e4u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1e4u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e4u" /> '''N-TERMINAL RING FINGER DOMAIN OF HUMAN NOT-...)
Line 1: Line 1:
-
[[Image:1e4u.gif|left|200px]]<br />
+
[[Image:1e4u.gif|left|200px]]<br /><applet load="1e4u" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1e4u" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1e4u" />
caption="1e4u" />
'''N-TERMINAL RING FINGER DOMAIN OF HUMAN NOT-4'''<br />
'''N-TERMINAL RING FINGER DOMAIN OF HUMAN NOT-4'''<br />
==Overview==
==Overview==
-
The NOT4 protein is a component of the CCR4.NOT complex, a global, regulator of RNA polymerase II transcription. Human NOT4 (hNOT4) contains, a RING finger motif of the C(4)C(4) type. We expressed and purified the, N-terminal region of hNOT4 (residues 1-78) encompassing the RING finger, motif and determined the solution structure by heteronuclear NMR. NMR, experiments using a (113)Cd-substituted hNOT4 RING finger showed that two, metal ions are bound through cysteine residues in a cross-brace manner., The three-dimensional structure of the hNOT4 RING finger was refined with, root mean square deviation values of 0.58 +/- 0.13 A for the backbone, atoms and 1.08 +/- 0.12 A for heavy atoms. The hNOT4 RING finger consists, of an alpha-helix and three long loops that are stabilized by zinc, coordination. The overall folding of the hNOT4 RING finger is similar to, that of the C(3)HC(4) RING fingers. The relative orientation of the two, zinc-chelating loops and the alpha-helix is well conserved. However, for, the other regions, the secondary structural elements are distinct.
+
The NOT4 protein is a component of the CCR4.NOT complex, a global regulator of RNA polymerase II transcription. Human NOT4 (hNOT4) contains a RING finger motif of the C(4)C(4) type. We expressed and purified the N-terminal region of hNOT4 (residues 1-78) encompassing the RING finger motif and determined the solution structure by heteronuclear NMR. NMR experiments using a (113)Cd-substituted hNOT4 RING finger showed that two metal ions are bound through cysteine residues in a cross-brace manner. The three-dimensional structure of the hNOT4 RING finger was refined with root mean square deviation values of 0.58 +/- 0.13 A for the backbone atoms and 1.08 +/- 0.12 A for heavy atoms. The hNOT4 RING finger consists of an alpha-helix and three long loops that are stabilized by zinc coordination. The overall folding of the hNOT4 RING finger is similar to that of the C(3)HC(4) RING fingers. The relative orientation of the two zinc-chelating loops and the alpha-helix is well conserved. However, for the other regions, the secondary structural elements are distinct.
==About this Structure==
==About this Structure==
-
1E4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1E4U OCA].
+
1E4U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1E4U OCA].
==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Albert, T.K.]]
+
[[Category: Albert, T K.]]
[[Category: Boelens, R.]]
[[Category: Boelens, R.]]
[[Category: Hanzawa, H.]]
[[Category: Hanzawa, H.]]
-
[[Category: Ruwe, M.J.De.]]
+
[[Category: Ruwe, M J.De.]]
-
[[Category: Timmers, H.Th M.]]
+
[[Category: Timmers, H Th M.]]
-
[[Category: Vliet, P.C.Van.Der.]]
+
[[Category: Vliet, P C.Van Der.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: transcriptional control]]
[[Category: transcriptional control]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:39:53 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:23:49 2008''

Revision as of 10:23, 21 February 2008


1e4u

Drag the structure with the mouse to rotate

N-TERMINAL RING FINGER DOMAIN OF HUMAN NOT-4

Overview

The NOT4 protein is a component of the CCR4.NOT complex, a global regulator of RNA polymerase II transcription. Human NOT4 (hNOT4) contains a RING finger motif of the C(4)C(4) type. We expressed and purified the N-terminal region of hNOT4 (residues 1-78) encompassing the RING finger motif and determined the solution structure by heteronuclear NMR. NMR experiments using a (113)Cd-substituted hNOT4 RING finger showed that two metal ions are bound through cysteine residues in a cross-brace manner. The three-dimensional structure of the hNOT4 RING finger was refined with root mean square deviation values of 0.58 +/- 0.13 A for the backbone atoms and 1.08 +/- 0.12 A for heavy atoms. The hNOT4 RING finger consists of an alpha-helix and three long loops that are stabilized by zinc coordination. The overall folding of the hNOT4 RING finger is similar to that of the C(3)HC(4) RING fingers. The relative orientation of the two zinc-chelating loops and the alpha-helix is well conserved. However, for the other regions, the secondary structural elements are distinct.

About this Structure

1E4U is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers., Hanzawa H, de Ruwe MJ, Albert TK, van Der Vliet PC, Timmers HT, Boelens R, J Biol Chem. 2001 Mar 30;276(13):10185-90. Epub 2000 Nov 21. PMID:11087754

Page seeded by OCA on Thu Feb 21 12:23:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools