| http://purl.uniprot.org/citations/21543860 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21543860 | http://www.w3.org/2000/01/rdf-schema#comment | "Effectors of the Rab small GTPases are large multi-domain proteins which have proved difficult to express in soluble form in Escherichia coli. Generally, effectors are recruited to a distinct subcellular compartment by active (GTP-bound) Rabs, which are linked to membranes by one or two prenylated Cys residues at their C-termini. Following recruitment via their Rab-binding domain (RBD), effectors carry out various aspects of vesicle formation, transport, tethering and fusion through their other domains. Previously, successful purification of the RUN-PLAT tandem domains (residues 683-1061) of the 1263-residue Rab6-interacting protein 1 (R6IP1) required co-expression with Rab6, as attempts to solubly express the effector alone were unsuccessful. R6IP1 is also known as DENN domain-containing protein 5 (DENND5) and is expressed as two isoforms, R6IP1A/B (DENND5A/B), which differ by 24 amino acids at the N-terminus. Here, a deletion in R6IP1 was engineered to enable soluble expression and to improve the quality of the crystals grown in complex with Rab6. A large 23-residue loop linking two α-helices in the RUN1 domain was removed and replaced with a short linker. This loop resides on the opposite face to the Rab6-binding site and is not conserved in the RUN-domain family. In contrast to wild-type R6IP1-Rab6 crystals, which took several weeks to grow to full size, the engineered R6IP1 (RPdel)-Rab6 crystals could be grown in a matter of days."xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.org/dc/terms/identifier | "doi:10.1107/s174430911100724x"xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/author | "Khan A.R."xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/author | "Fernandes H."xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/author | "Franklin E."xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/name | "Acta Crystallogr Sect F Struct Biol Cryst Commun"xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/pages | "556-560"xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/title | "Crystallization of an engineered RUN domain of Rab6-interacting protein 1/DENND5."xsd:string |
| http://purl.uniprot.org/citations/21543860 | http://purl.uniprot.org/core/volume | "67"xsd:string |
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