1z09: Difference between revisions

Revision as of 05:40, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z09.png

Template:STRUCTURE 1z09

Solution structure of km23Solution structure of km23

Template:ABSTRACT PUBMED 16083906

About this StructureAbout this Structure

1Z09 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Structure and dynamics of the homodimeric dynein light chain km23., Ilangovan U, Ding W, Zhong Y, Wilson CL, Groppe JC, Trbovich JT, Zuniga J, Demeler B, Tang Q, Gao G, Mulder KM, Hinck AP, J Mol Biol. 2005 Sep 16;352(2):338-54. PMID:16083906

Page seeded by OCA on Tue Jul 29 05:40:04 2008

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OCA

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-[[Image:1z09.gif|left|200px]]
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 {{STRUCTURE_1z09|  PDB=1z09  |  SCENE=  }}
-'''Solution structure of km23'''
+===Solution structure of km23===
-==Overview==
+<!--
-km23 (96 residues, 11 kDa) is the mammalian ortholog of Drosophila roadblock, the founding member of LC7/robl/km23 class of dynein light chains. km23 has been shown to be serine-phosphorylated following TGFbeta receptor activation and to bind the dynein intermediate chain in response to such phosphorylation. Here, we report the three-dimensional solution structure of km23, which is shown to be that of a homodimer, similar to that observed for the heterodimeric complex formed between p14 and MP1, two distantly related members of the MglB/robl superfamily, but distinct from the LC8 and Tctex-1 classes of dynein light chains, which also adopt homodimeric structures. The conserved surface residues of km23, including three serine residues, are located predominantly on a single face of the molecule. Adjacent to this face is a large cleft formed by the incomplete overlap of loops from opposite monomers. As shown by NMR relaxation data collected at two fields, several cleft residues are flexible on the ns-ps and ms-mus timescales. Based on these observations, we propose that the patch of conserved residues on the central face of the molecule corresponds to the site at which km23 binds the dynein intermediate chain and that the flexible cleft formed between the overlap of loops from the two monomers corresponds to the site at which km23 binds other partners, such as the TGFbeta type II receptor or Smad2.
+The line below this paragraph, {{ABSTRACT_PUBMED_16083906}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16083906 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16083906}}
 ==About this Structure==
-Z09 is a [[Single protein]] structure of sequence 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=1Z09 OCA].
+Z09 is a [[Single protein]] structure of sequence 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=1Z09 OCA].
 ==Reference==
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 [[Category: Lc7]]
 [[Category: Protein-protein complex]]
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