dc.contributor.author | Sporny, M | |
dc.contributor.author | Guez-Haddad, J | |
dc.contributor.author | Waterman, DG | |
dc.contributor.author | Isupov, MN | |
dc.contributor.author | Opatowsky, Y | |
dc.date.accessioned | 2018-07-19T07:19:52Z | |
dc.date.issued | 2016-10 | |
dc.description.abstract | SRGAP2 (Slit-Robo GTPase-activating protein 2) is a cytoplasmic protein found to be involved in neuronal branching, restriction of neuronal migration and restriction of the length and density of dendritic postsynaptic spines. The extended F-BAR (F-BARx) domain of SRGAP2 generates membrane protrusions when expressed in COS-7 cells, while most F-BARs induce the opposite effect: membrane invaginations. As a first step to understand this discrepancy, the F-BARx domain of SRGAP2 was isolated and crystallized after co-expression with the carboxy domains of the protein. Diffraction data were collected from two significantly non-isomorphous crystals in the same monoclinic C2 space group. A correct molecular-replacment solution was obtained by applying a molecular symmetry-constrained systematic search approach that took advantage of the conserved biological symmetry of the F-BAR domains. It is shown that similar approaches can solve other F-BAR structures that were previously determined by experimental phasing. Diffraction data were reprocessed with a high-resolution cutoff of 2.2 Å, chosen using less strict statistical criteria. This has improved the outcome of multi-crystal averaging and other density-modification procedures. | en_GB |
dc.description.sponsorship | This work was supported by funds from the ISF (Grant No. 1425/15 to YO) and BSF (Grant No.
2013310 to YO). | en_GB |
dc.identifier.citation | Vol. 72, pp. 1241 - 1253 | en_GB |
dc.identifier.doi | 10.1107/S2059798316016697 | |
dc.identifier.other | S2059798316016697 | |
dc.identifier.uri | http://hdl.handle.net/10871/33489 | |
dc.language.iso | en | en_GB |
dc.publisher | International Union of Crystallography | en_GB |
dc.relation.url | https://www.ncbi.nlm.nih.gov/pubmed/27917825 | en_GB |
dc.rights | (C) 2016 International Union of Crystallography | en_GB |
dc.subject | F-BAR | en_GB |
dc.subject | SRGAP2 | en_GB |
dc.subject | coiled coil | en_GB |
dc.subject | exhaustive search | en_GB |
dc.subject | molecular replacement | en_GB |
dc.subject | Animals | en_GB |
dc.subject | COS Cells | en_GB |
dc.subject | Cercopithecus aethiops | en_GB |
dc.subject | Crystallography, X-Ray | en_GB |
dc.subject | GTPase-Activating Proteins | en_GB |
dc.subject | Humans | en_GB |
dc.subject | Models, Molecular | en_GB |
dc.subject | Protein Conformation, alpha-Helical | en_GB |
dc.subject | Protein Domains | en_GB |
dc.title | Molecular symmetry-constrained systematic search approach to structure solution of the coiled-coil SRGAP2 F-BARx domain. | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2018-07-19T07:19:52Z | |
dc.identifier.issn | 2059-7983 | |
exeter.place-of-publication | United States | en_GB |
dc.description | This is the final version of the article. Available from International Union of Crystallography via the DOI in this record. | en_GB |
dc.identifier.journal | Acta Crystallographica. Section d, Structural Biology | en_GB |