1f95

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[[Image:1f95.gif|left|200px]]<br /><applet load="1f95" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1f95" />
 
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'''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX'''<br />
 
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==Overview==
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==SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX==
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Dyneins are multi-subunit molecular motors that translocate molecular cargoes along microtubules. Other than acting as an essential component of the dynein motor complex, the 89-residue subunit of dynein light chain (DLC8) also regulates a number of other biological events by binding to various proteins and enzymes. Currently known DLC8 targets include neuronal nitric oxide synthase; the proapoptotic Bcl-2 family member protein designated Bim; a Drosophila RNA localization protein Swallow, myosin V, neuronal scaffolding protein GKAP, and IkappaBalpha, an inhibitor of the NFkappaB transcription factor. The DLC8-binding domains of the various targets are confined within a short, continuous stretch of amino acid residues. However, these domains do not share any obvious sequence homology with each other. Here, the three-dimensional structures of DLC8 complexed with two peptides corresponding to the DLC8-binding domains of neuronal nitric oxide synthase and Bim, respectively, were determined by NMR spectroscopy. Although the two DLC8-binding peptides have entirely different amino acid sequences, both peptides bind to the protein with a remarkable similar conformation by engaging the symmetric DLC8 dimer through antiparallel beta-sheet augmentation via the beta2 strand of the protein. Structural comparison indicates that the two target peptides use different regions within the conformational flexible peptide-binding channels to achieve binding specificity. We have also re-determined the apo-form solution structure of DLC8 in this work. The structures of the DLC8/target peptide complexes, together with the dynamic properties of the protein, provide a molecular basis of DLC8's diverse amino acid sequence-dependent target recognition.
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<StructureSection load='1f95' size='340' side='right'caption='[[1f95]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1f95]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F95 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f95 OCA], [https://pdbe.org/1f95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f95 RCSB], [https://www.ebi.ac.uk/pdbsum/1f95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f95 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DYL1_RAT DYL1_RAT] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures. Binds and inhibits the catalytic activity of neuronal nitric oxide synthase. Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 (By similarity). Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/1f95_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f95 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1F95 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F95 OCA].
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*[[Dynein 3D structures|Dynein 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain., Fan J, Zhang Q, Tochio H, Li M, Zhang M, J Mol Biol. 2001 Feb 9;306(1):97-108. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11178896 11178896]
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[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Fan, J S.]]
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[[Category: Fan J-S]]
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[[Category: Li, M.]]
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[[Category: Li M]]
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[[Category: Tochio, H.]]
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[[Category: Tochio H]]
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[[Category: Zhang, M.]]
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[[Category: Zhang M]]
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[[Category: Zhang, Q.]]
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[[Category: Zhang Q]]
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[[Category: bim]]
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[[Category: dlc8]]
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[[Category: dynein]]
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[[Category: light chain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:10 2008''
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Current revision

SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX

PDB ID 1f95

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