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5yza

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Current revision (10:25, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5yza' size='340' side='right'caption='[[5yza]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5yza' size='340' side='right'caption='[[5yza]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yza]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YZA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yza]] 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=5YZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZA FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yza OCA], [http://pdbe.org/5yza PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yza RCSB], [http://www.ebi.ac.uk/pdbsum/5yza PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yza ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=5yza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yza OCA], [https://pdbe.org/5yza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yza RCSB], [https://www.ebi.ac.uk/pdbsum/5yza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yza ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DPYL2_HUMAN DPYL2_HUMAN]] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in neuron projection morphogenesis.<ref>PMID:11477421</ref> <ref>PMID:15466863</ref>
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[https://www.uniprot.org/uniprot/DPYL2_HUMAN DPYL2_HUMAN] Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in neuron projection morphogenesis.<ref>PMID:11477421</ref> <ref>PMID:15466863</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Collapsin response mediator protein 2 (CRMP2) regulates neuronal polarity by controlling microtubule dynamics. CRMP2 activity is regulated by semaphorin-induced phosphorylation at the C-terminal tail domain. Unphosphorylated CRMP2 induces effective axonal microtubule formation to give the axonal characteristics to a neurite, whereas phosphorylated CRMP2 leads to the apparently opposite effect, growth cone collapse. We have recently characterized the structural detail of CRMP2-induced axonal microtubule formation (Niwa et al. (2017) Sci. Rep., 7: 10681). CRMP2 forms the hetero-trimer with GTP-tubulin to induce effective axonal microtubule formation in the future axon. Phosphorylation of CRMP2 has been reported to decrease the affinity between CRMP2 and the microtubule, albeit the molecular mechanisms of how the phosphorylation of CRMP2 changes the structure to achieve distinct effects from unphosphorylated CRMP2 is not well understood. Here we performed a series of biochemical and structural analyses of phospho-mimic CRMP2. Phosphorylation of CRMP2 undergoes small conformational changes at the C-terminal tail with shifting the surface charge, which not only alters the interactions within the CRMP2 tetramer but also alters the interactions with GTP-tubulin. Consequently, phospho-mimic CRMP2 fails to form a hetero-trimer with GTP-tubulin, thus losing the ability to establish and maintain the axonal microtubules.Key words: CRMP2, phosphorylation, microtubule, axon, crystal structure.
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Structural Insights into the Altering Function of CRMP2 by Phosphorylation.,Sumi T, Imasaki T, Aoki M, Sakai N, Nitta E, Shirouzu M, Nitta R Cell Struct Funct. 2018;43(1):15-23. doi: 10.1247/csf.17025. PMID:29479005<ref>PMID:29479005</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5yza" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Aoki, M]]
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[[Category: Aoki M]]
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[[Category: Imasaki, T]]
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[[Category: Imasaki T]]
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[[Category: Nitta, E]]
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[[Category: Nitta E]]
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[[Category: Nitta, R]]
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[[Category: Nitta R]]
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[[Category: Sakai, N]]
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[[Category: Sakai N]]
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[[Category: Shirouzu, M]]
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[[Category: Shirouzu M]]
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[[Category: Sumi, T]]
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[[Category: Sumi T]]
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[[Category: Collapsin response]]
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[[Category: Cytosolic protein]]
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[[Category: Developmental protein]]
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[[Category: Neurogenesi related protein]]
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[[Category: Phosphop associated protein]]
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[[Category: Protein binding]]
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Current revision

Crystal Structure of Human CRMP-2 with S522D mutation

PDB ID 5yza

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