1y4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1y4o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4o" /> '''Solution structure of a mouse cytoplasmic Ro...)
Line 1: Line 1:
-
[[Image:1y4o.gif|left|200px]]<br /><applet load="1y4o" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1y4o.gif|left|200px]]<br /><applet load="1y4o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1y4o" />
caption="1y4o" />
'''Solution structure of a mouse cytoplasmic Roadblock/LC7 dynein light chain'''<br />
'''Solution structure of a mouse cytoplasmic Roadblock/LC7 dynein light chain'''<br />
==Overview==
==Overview==
-
Roadblock/LC7 is a member of a class of dynein light chains involved in, regulating the function of the dynein complex. We have determined the, three-dimensional structure of isoform 1 of the mouse Roadblock/LC7, cytoplasmic dynein light chain (robl1_mouse) by NMR spectroscopy. In, contrast to a previously reported NMR structure of the human homolog with, 96% sequence identity (PDB 1TGQ), which showed the protein as a monomer, our results indicate clearly that robl1 exists as a symmetric homodimer., The two beta3-strands pair with each other and form a continuous, ten-stranded beta-sheet. The 25-residue alpha2-helix from one subunit, packs antiparallel to that of the other subunit on the face of the, beta-sheet. Zipper-like hydrophobic contacts between the two helices serve, to stabilize the dimer. Through an NMR titration experiment, we localized, the site on robl1_mouse that interacts with the 40 residue peptide, spanning residues 243 through 282 of IC74-1_rat. These results provide, physical evidence for a symmetrical interaction between dimeric robl1 and, the two molecules of IC74-1 in the dynein complex.
+
Roadblock/LC7 is a member of a class of dynein light chains involved in regulating the function of the dynein complex. We have determined the three-dimensional structure of isoform 1 of the mouse Roadblock/LC7 cytoplasmic dynein light chain (robl1_mouse) by NMR spectroscopy. In contrast to a previously reported NMR structure of the human homolog with 96% sequence identity (PDB 1TGQ), which showed the protein as a monomer, our results indicate clearly that robl1 exists as a symmetric homodimer. The two beta3-strands pair with each other and form a continuous ten-stranded beta-sheet. The 25-residue alpha2-helix from one subunit packs antiparallel to that of the other subunit on the face of the beta-sheet. Zipper-like hydrophobic contacts between the two helices serve to stabilize the dimer. Through an NMR titration experiment, we localized the site on robl1_mouse that interacts with the 40 residue peptide spanning residues 243 through 282 of IC74-1_rat. These results provide physical evidence for a symmetrical interaction between dimeric robl1 and the two molecules of IC74-1 in the dynein complex.
==About this Structure==
==About this Structure==
-
1Y4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y4O OCA].
+
1Y4O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y4O OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: CESG, Center.for.Eukaryotic.Structural.Genomics.]]
+
[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
-
[[Category: Lee, M.S.]]
+
[[Category: Lee, M S.]]
-
[[Category: Markley, J.L.]]
+
[[Category: Markley, J L.]]
[[Category: Song, J.]]
[[Category: Song, J.]]
-
[[Category: Tyler, E.M.]]
+
[[Category: Tyler, E M.]]
-
[[Category: Tyler, R.C.]]
+
[[Category: Tyler, R C.]]
[[Category: center for eukaryotic structural genomics]]
[[Category: center for eukaryotic structural genomics]]
[[Category: cesg]]
[[Category: cesg]]
Line 26: Line 26:
[[Category: structural genomics]]
[[Category: structural genomics]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:33:55 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:45 2008''

Revision as of 14:01, 21 February 2008


1y4o

Drag the structure with the mouse to rotate

Solution structure of a mouse cytoplasmic Roadblock/LC7 dynein light chain

Overview

Roadblock/LC7 is a member of a class of dynein light chains involved in regulating the function of the dynein complex. We have determined the three-dimensional structure of isoform 1 of the mouse Roadblock/LC7 cytoplasmic dynein light chain (robl1_mouse) by NMR spectroscopy. In contrast to a previously reported NMR structure of the human homolog with 96% sequence identity (PDB 1TGQ), which showed the protein as a monomer, our results indicate clearly that robl1 exists as a symmetric homodimer. The two beta3-strands pair with each other and form a continuous ten-stranded beta-sheet. The 25-residue alpha2-helix from one subunit packs antiparallel to that of the other subunit on the face of the beta-sheet. Zipper-like hydrophobic contacts between the two helices serve to stabilize the dimer. Through an NMR titration experiment, we localized the site on robl1_mouse that interacts with the 40 residue peptide spanning residues 243 through 282 of IC74-1_rat. These results provide physical evidence for a symmetrical interaction between dimeric robl1 and the two molecules of IC74-1 in the dynein complex.

About this Structure

1Y4O is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex., Song J, Tyler RC, Lee MS, Tyler EM, Markley JL, J Mol Biol. 2005 Dec 16;354(5):1043-51. Epub 2005 Nov 2. PMID:16289575

Page seeded by OCA on Thu Feb 21 16:01:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools