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Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7.
DC Field | Value | Language |
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dc.contributor.author | Han, D | - |
dc.contributor.author | Kim, K | - |
dc.contributor.author | Kim, Y | - |
dc.contributor.author | Kang, Y | - |
dc.contributor.author | Lee, JY | - |
dc.date.accessioned | 2010-11-30T01:45:17Z | - |
dc.date.available | 2010-11-30T01:45:17Z | - |
dc.date.issued | 2009 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://repository.ajou.ac.kr/handle/201003/342 | - |
dc.description.abstract | Anaphase-promoting complex or cyclosome (APC/C) is an unusual E3 ubiquitin ligase and an essential protein that controls mitotic progression. APC/C includes at least 13 subunits, but no structure has been determined for any tetratricopeptide repeat (TPR)-containing subunit (Apc3 and -6-8) in the TPR subcomplex of APC/C. Apc7 is a TPR-containing subunit that exists only in vertebrate APC/C. Here we report the crystal structure of quad mutant of nApc7 (N-terminal fragment, residues 1-147) of human Apc7 at a resolution of 2.5 A. The structure of nApc7 adopts a TPR-like motif and has a unique dimerization interface, although the protein does not contain the conserved TPR sequence. Based on the structure of nApc7, in addition to previous experimental findings, we proposed a putative homodimeric structure for full-length Apc7. This model suggests that TPR-containing subunits self-associate and bind to adaptors and substrates via an IR peptide in TPR-containing subunits of APC/C. | - |
dc.language.iso | en | - |
dc.subject.MESH | Amino Acid Motifs | - |
dc.subject.MESH | Amino Acid Sequence | - |
dc.subject.MESH | Crystallography, X-Ray | - |
dc.subject.MESH | Humans | - |
dc.subject.MESH | Models, Molecular | - |
dc.subject.MESH | Molecular Sequence Data | - |
dc.subject.MESH | Peptide Fragments | - |
dc.subject.MESH | Pliability | - |
dc.subject.MESH | Protein Multimerization | - |
dc.subject.MESH | Protein Structure, Tertiary | - |
dc.subject.MESH | Protein Subunits | - |
dc.subject.MESH | Repetitive Sequences, Amino Acid | - |
dc.subject.MESH | Sequence Alignment | - |
dc.subject.MESH | Sequence Homology, Amino Acid | - |
dc.subject.MESH | Ubiquitin-Protein Ligase Complexes | - |
dc.title | Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7. | - |
dc.type | Article | - |
dc.identifier.pmid | 19091741 | - |
dc.identifier.url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2685695/ | - |
dc.contributor.affiliatedAuthor | 강, 엽 | - |
dc.type.local | Journal Papers | - |
dc.identifier.doi | 10.1074/jbc.M804887200 | - |
dc.citation.title | The Journal of biological chemistry | - |
dc.citation.volume | 284 | - |
dc.citation.number | 22 | - |
dc.citation.date | 2009 | - |
dc.citation.startPage | 15137 | - |
dc.citation.endPage | 15146 | - |
dc.identifier.bibliographicCitation | The Journal of biological chemistry, 284(22). : 15137-15146, 2009 | - |
dc.identifier.eissn | 1083-351X | - |
dc.relation.journalid | J000219258 | - |
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