View source for 4b92


==Crystal structure of truncated human CRMP-5 soaked with Zn==
<StructureSection load='4b92' size='340' side='right'caption='[[4b92]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4b92]] 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=4B92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B92 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4b92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b92 OCA], [https://pdbe.org/4b92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b92 RCSB], [https://www.ebi.ac.uk/pdbsum/4b92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b92 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPYL5_HUMAN DPYL5_HUMAN] May have a function in neuronal differentiation and/or axon growth.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Collapsin Response Mediator Protein-5 (CRMP-5) is the latest identified member of the CRMP cytosolic phosphoprotein family, which is crucial for neuronal development and repair. CRMPs exist as homo- and/or hetero-tetramers in vivo and participate in signaling transduction, cytoskeleton rearrangements, and endocytosis. CRMP-5 antagonizes many of the other CRMPs' functions either by directly interacting with them or by competing for their binding partners. We determined the crystal structures of a full length and a truncated version of human CRMP-5, both of which form a homo-tetramer similar to those observed in CRMP-1 and CRMP-2. However, solution studies indicate that CRMP-5 and CRMP-1 form weaker homo-tetramers compared to CRMP-2, and that divalent cations, Ca(2+) and Mg(2+) , destabilize oligomers of CRMP-5 and CRMP-1, but promote CRMP-2 oligomerization. Based on comparative analysis of the CRMP-5 crystal structure we identified residues that are crucial for determining the preference for hetero-oligomer or homo-oligomer formation. We also show that in spite of being the CRMP family member most closely related to dihydropyrimidinase, CRMP-5 does not have any detectable amidohydrolase activity. The presented findings provide new detailed insights into the structure, oligomerization and regulation of CRMPs. (c) 2013 International Society for Neurochemistry, J. Neurochem. (2013) 10.1111/jnc.12188.

Insights into the oligomerization of CRMPs: Crystal structure of human collapsin response mediator protein 5.,Ponnusamy R, Lohkamp B J Neurochem. 2013 Feb 4. doi: 10.1111/jnc.12188. PMID:23373749<ref>PMID:23373749</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4b92" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Lohkamp B]]
[[Category: Ponnusamy R]]