4CNS
Crystal structure of truncated human CRMP-4
Summary for 4CNS
| Entry DOI | 10.2210/pdb4cns/pdb |
| Related | 4CNT 4CNU |
| Descriptor | DIHYDROPYRIMIDINASE-LIKE 3, 1,2-ETHANEDIOL, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | signaling protein, neurogenesis, axonal outgrowth, developmental protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 4 |
| Total formula weight | 211081.66 |
| Authors | Ponnusamy, R.,Lohkamp, B. (deposition date: 2014-01-24, release date: 2014-06-18, Last modification date: 2023-12-20) |
| Primary citation | Ponnusamy, R.,Lebedev, A.,Pahlow, S.,Lohkamp, B. Crystal Structure of Human Crmp-4: Correction of Intensities for Lattice-Translocation Disorder Acta Crystallogr.,Sect.D, 70:1680-, 2014 Cited by PubMed Abstract: 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. PubMed: 24914979DOI: 10.1107/S1399004714006634 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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