View source for 4cnu


==CRYSTAL STRUCTURE OF WT HUMAN CRMP-4 from lattice translocation==
<StructureSection load='4cnu' size='340' side='right'caption='[[4cnu]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cnu]] 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=4CNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CNU 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]] 2.8&#8491;</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=4cnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cnu OCA], [https://pdbe.org/4cnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cnu RCSB], [https://www.ebi.ac.uk/pdbsum/4cnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cnu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPYL3_HUMAN DPYL3_HUMAN] Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity).
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== Publication Abstract from PubMed ==
Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins that are mainly involved in neuronal cell development. In humans, the CRMP family comprises five members. Here, crystal structures of human CRMP-4 in a truncated and a full-length version are presented. The latter was determined from two types of crystals, which were either twinned or partially disordered. The crystal disorder was coupled with translational NCS in ordered domains and manifested itself with a rather sophisticated modulation of intensities. The data were demodulated using either the two-lattice treatment of lattice-translocation effects or a novel method in which demodulation was achieved by independent scaling of several groups of intensities. This iterative protocol does not rely on any particular parameterization of the modulation coefficients, but uses the current refined structure as a reference. The best results in terms of R factors and map correlation coefficients were obtained using this new method. The determined structures of CRMP-4 are similar to those of other CRMPs. Structural comparison allowed the confirmation of known residues, as well as the identification of new residues, that are important for the homo- and hetero-oligomerization of these proteins, which are critical to nerve-cell development. The structures provide further insight into the effects of medically relevant mutations of the DPYSL-3 gene encoding CRMP-4 and the putative enzymatic activities of CRMPs.

Crystal structure of human CRMP-4: correction of intensities for lattice-translocation disorder.,Ponnusamy R, Lebedev AA, Pahlow S, Lohkamp B Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1680-94. doi:, 10.1107/S1399004714006634. Epub 2014 May 30. PMID:24914979<ref>PMID:24914979</ref>

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