| http://purl.uniprot.org/citations/33989636 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33989636 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33989636 | http://www.w3.org/2000/01/rdf-schema#comment | "Tripartite motif (TRIM)7 is an E3 ubiquitin ligase that was first identified through its interaction with glycogenin-1 (GN1), the autoglucosyltransferase that initiates glycogen biosynthesis. A growing body of evidence indicates that TRIM7 plays an important role in cancer development, viral pathogenesis, and atherosclerosis and, thus, represents a potential therapeutic target. TRIM family proteins share a multidomain architecture with a conserved N-terminal TRIM and a variable C-terminal domain. Human TRIM7 contains the canonical TRIM motif and a B30.2 domain at the C terminus. To contribute to the understanding of the mechanism of action of TRIM7, we solved the X-ray crystal structure of its B30.2 domain (TRIM7B30.2) in two crystal forms at resolutions of 1.6 Å and 1.8 Å. TRIM7B30.2 exhibits the typical B30.2 domain fold, consisting of two antiparallel β-sheets of seven and six strands, arranged as a distorted β-sandwich. Furthermore, two long loops partially cover the concave face of the β-sandwich defined by the β-sheet of six strands, thus forming a positively charged cavity. We used sequence conservation and mutational analyses to provide evidence of a putative binding interface for GN1. These studies showed that Leu423, Ser499, and Cys501 of TRIM7B30.2 and the C-terminal 33 amino acids of GN1 are critical for this binding interaction. Molecular dynamics simulations also revealed that hydrogen bond and hydrophobic interactions play a major role in the stability of a modeled TRIM7B30.2-GN1 C-terminal peptide complex. These data provide useful information that could be used to target this interaction for the development of potential therapeutic agents."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jbc.2021.100772"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.jbc.2021.100772"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Carrizo M.E."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Carrizo M.E."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Issoglio F.M."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Issoglio F.M."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Munoz Sosa C.J."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/author | "Munoz Sosa C.J."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/pages | "100772"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/pages | "100772"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/title | "Crystal structure and mutational analysis of the human TRIM7 B30.2 domain provide insights into the molecular basis of its binding to glycogenin-1."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/title | "Crystal structure and mutational analysis of the human TRIM7 B30.2 domain provide insights into the molecular basis of its binding to glycogenin-1."xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/volume | "296"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://purl.uniprot.org/core/volume | "296"xsd:string |
| http://purl.uniprot.org/citations/33989636 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33989636 |
| http://purl.uniprot.org/citations/33989636 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33989636 |
| http://purl.uniprot.org/citations/33989636 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33989636 |
| http://purl.uniprot.org/citations/33989636 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33989636 |