This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4dkk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:50, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer==
==The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer==
-
<StructureSection load='4dkk' size='340' side='right' caption='[[4dkk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+
<StructureSection load='4dkk' size='340' side='right'caption='[[4dkk]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4dkk]] is a 1 chain structure with 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=4DKK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DKK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4dkk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DKK FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.701&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STAU, STAU1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dkk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dkk RCSB], [http://www.ebi.ac.uk/pdbsum/4dkk PDBsum]</span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dkk OCA], [https://pdbe.org/4dkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dkk RCSB], [https://www.ebi.ac.uk/pdbsum/4dkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dkk ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/STAU1_HUMAN STAU1_HUMAN] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
-
Staufen1 (STAU1)-mediated mRNA decay (SMD) degrades mammalian-cell mRNAs that bind the double-stranded RNA (dsRNA)-binding protein STAU1 in their 3' untranslated region. We report a new motif, which typifies STAU homologs from all vertebrate classes, that is responsible for human STAU1 (hSTAU1) homodimerization. Our crystal structure and mutagenesis analyses reveal that this motif, which we named the Staufen-swapping motif (SSM), and the dsRNA-binding domain 5 ('RBD'5) mediate protein dimerization: the two SSM alpha-helices of one molecule interact primarily through a hydrophobic patch with the two 'RBD'5 alpha-helices of a second molecule. 'RBD'5 adopts the canonical alpha-beta-beta-beta-alpha fold of a functional RBD, but it lacks residues and features required to bind duplex RNA. In cells, SSM-mediated hSTAU1 dimerization increases the efficiency of SMD by augmenting hSTAU1 binding to the ATP-dependent RNA helicase hUPF1. Dimerization regulates keratinocyte-mediated wound healing and many other cellular processes.
+
-
 
+
-
Staufen1 dimerizes through a conserved motif and a degenerate dsRNA-binding domain to promote mRNA decay.,Gleghorn ML, Gong C, Kielkopf CL, Maquat LE Nat Struct Mol Biol. 2013 Apr;20(4):515-24. doi: 10.1038/nsmb.2528. Epub 2013 Mar, 24. PMID:23524536<ref>PMID:23524536</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Gleghorn, M L]]
+
[[Category: Large Structures]]
-
[[Category: Beta sheet]]
+
[[Category: Gleghorn ML]]
-
[[Category: Dimerization]]
+
-
[[Category: Protein binding]]
+
-
[[Category: Rbd]]
+
-
[[Category: Rna binding protein]]
+
-
[[Category: Swapping-motif]]
+

Current revision

The X-ray Crystal Structure of the Human STAU1 SSM-'RBD'5 Domain-Swapped Dimer

PDB ID 4dkk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4dkk"
Personal tools