| http://purl.uniprot.org/citations/15788412 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15788412 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15788412 | http://www.w3.org/2000/01/rdf-schema#comment | "Vacuolar protein sorting protein 29 (Vps29p), which is involved in retrograde trafficking from prevacuolar endosomes to the trans-Golgi network, performs its biological functions by participating in the formation of a "retromer complex." In human cells, this complex comprises four conserved proteins: hVps35p, hVps29p, hVps26p, and sorting nexin 1 protein (SNX1). Here, we report the crystal structure of hVps29p at 2.1 Angstroms resolution, the first three-dimensional structure of the retromer subunits. This novel structure adopts a four-layered alpha-beta-beta-alpha sandwich fold. hVps29p contains a metal-binding site that is very similar to the active sites of some proteins of the phosphodiesterase/nuclease protein family, indicating that hVps29p may carry out chemically similar functions. Structure and sequence conservation analysis suggests that hVps29p contains two protein-protein interaction sites. One site, which potentially serves as the interface between hVps29p and hVps35p, comprises 5 conserved hydrophobic and 8 hydrophilic residues. The other site is relatively more hydrophilic and may serve as a binding interface with hVps26p, SNX1, or other target proteins."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m500464200"xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m500464200"xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Dong Y."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Dong Y."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Fan J."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Fan J."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Guo M."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Guo M."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Li X."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Li X."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Liu P."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Liu P."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Niu L."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Niu L."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Zhu Z."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Zhu Z."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Teng M."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Teng M."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Zang J."xsd:string |
| http://purl.uniprot.org/citations/15788412 | http://purl.uniprot.org/core/author | "Zang J."xsd:string |