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| | ==Crystal Structure of Human CRMP-2 without C-terminal Tail== | | ==Crystal Structure of Human CRMP-2 without C-terminal Tail== |
| - | <StructureSection load='5x1c' size='340' side='right' caption='[[5x1c]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5x1c' size='340' side='right'caption='[[5x1c]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x1c]] is a 2 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=5X1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X1C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x1a|5x1a]], [[5x1d|5x1d]]</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]] 2.101Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DPYSL2, CRMP2, ULIP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5x1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1c OCA], [https://pdbe.org/5x1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x1c RCSB], [https://www.ebi.ac.uk/pdbsum/5x1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1c ProSAT]</span></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=5x1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x1c OCA], [http://pdbe.org/5x1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x1c RCSB], [http://www.ebi.ac.uk/pdbsum/5x1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x1c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [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> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Microtubule associated protein Collapsin response mediator protein 2 (CRMP2) regulates neuronal polarity in developing neurons through interactions with tubulins or microtubules. However, how CRMP2 promotes axonal formation by affecting microtubule behavior remains unknown. This study aimed to obtain the structural basis for CRMP2-tubulin/microtubule interaction in the course of axonogenesis. The X-ray structural studies indicated that the main interface to the soluble tubulin-dimer is the last helix H19 of CRMP2 that is distinct from the known C-terminal tail-mediated interaction with assembled microtubules. In vitro structural and functional studies also suggested that the H19-mediated interaction promoted the rapid formation of GTP-state microtubules directly, which is an important feature of the axon. Consistently, the H19 mutants disturbed axon elongation in chick neurons, and failed to authorize the structural features for axonal microtubules in Caenorhabditis elegans. Thus, CRMP2 induces effective axonal microtubule formation through H19-mediated interactions with a soluble tubulin-dimer allowing axonogenesis to proceed.
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| - | Structural basis for CRMP2-induced axonal microtubule formation.,Niwa S, Nakamura F, Tomabechi Y, Aoki M, Shigematsu H, Matsumoto T, Yamagata A, Fukai S, Hirokawa N, Goshima Y, Shirouzu M, Nitta R Sci Rep. 2017 Sep 6;7(1):10681. doi: 10.1038/s41598-017-11031-4. PMID:28878401<ref>PMID:28878401</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5x1c" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Aoki, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Nitta, R]] | + | [[Category: Aoki M]] |
| - | [[Category: Shirouzu, M]] | + | [[Category: Nitta R]] |
| - | [[Category: Tomabechi, Y]] | + | [[Category: Shirouzu M]] |
| - | [[Category: Collapsin response mediator protein]]
| + | [[Category: Tomabechi Y]] |
| - | [[Category: Developmental protein]]
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| - | [[Category: Dihydropyrimidase-related protein]]
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| - | [[Category: Microtubule associated protein]]
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| - | [[Category: Neurogenesis]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Protein binding]]
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