NMR structure of Lys48-linked di-ubiquitin using chemical shift perturbation data together with RDCs and 15N-relaxation data
Various Strategies of Using Residual Dipolar Couplings in NMR-Driven Protein Docking: Application to Lys48-Linked Di-Ubiquitin and Validation Against 15N-Relaxation Data
Structural Properties of Polyubiquitin Chains in Solution
ISOPEPTIDE BOND BETWEEN GLY76A AND LYS48B
MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN
MECHANISM OF UBIQUITIN RECOGNITION BY THE CUE DOMAIN OF VPS9
A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN
FUNCTIONS INCLUDE ATP-DEPENDENT SELECTIVE DEGRADATION OF CELLULAR PROTEINS, MAINTENANCE OF CHROMATIN STRUCTURE, REGULATION OF GENE EXPRESSION, STRESS RESPONSE, AND RIBOSOME BIOGENESIS
THE STRUCTURE WAS DETERMINED WITH HADDOCK USING CHEMICAL SHIFT PERTURBATION DATA AS AMBIGUOUS INTERACTION RESTRAINTS AND RESIDUAL DIPOLAR COUPLINGS BOTH AS DIRECT RESTRAINTS (SANI) AND INTERVECTOR PROJECTION ANGLE RESTRAINTS (VEAN). STRUCTURAL CHARACTERISTICS OF ENSEMBLE OF 10 BEST: AVERAGE (STANDARD DEVIATION) INTERMOLECULAR ENERGIES RAMACHANDRAN ANALYSIS:
LOWEST ENERGY STRUCTURES OF LOWEST ENERGY CLUSTER
REFINEMENT IS DONE IN EXPLICIT SOLVENT. REFINEMENT AND STRUCTURE CALCULATION DETAILS CAN BE FOUND IN DOMINGUEZ ET AL, JACS 2003, 125, 173
PROTEASOME, DEGRADATION, UBIQUITIN, POLYUBIQUITIN