1AAR
STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)
Summary for 1AAR
Entry DOI | 10.2210/pdb1aar/pdb |
Descriptor | DI-UBIQUITIN (2 entities in total) |
Functional Keywords | ubiquitin |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 2 |
Total formula weight | 17153.66 |
Authors | Cook, W.J.,Jeffrey, L.C.,Carson, M.,Chen, Z.,Pickart, C.M. (deposition date: 1992-04-17, release date: 1993-10-31, Last modification date: 2024-10-23) |
Primary citation | Cook, W.J.,Jeffrey, L.C.,Carson, M.,Chen, Z.,Pickart, C.M. Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). J.Biol.Chem., 267:16467-16471, 1992 Cited by PubMed Abstract: Covalent ligation of multiubiquitin chains targets eukaryotic proteins for degradation. In such multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of Gly76. The crystal structure of a diubiquitin conjugate has been determined and refined at 2.3-A resolution. The molecule has internal approximate 2-fold symmetry with multiple hydrophobic and hydrophilic contacts along the 2-fold axis. The structure of the diubiquitin conjugate suggests determinants for recognition of multiubiquitin chains. A model for the interaction of diubiquitin and a ubiquitin conjugating enzyme (E2) is proposed. PubMed: 1322903PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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