Structure of human TSG101 UEV domain
| Autor: | Ana Cámara-Artigas, Pedro L. Mateo, Andrés Palencia, Irene Luque, Jose C. Martinez |
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| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Stereochemistry Molecular Sequence Data Peptide macromolecular substances Crystal structure Crystallography X-Ray DNA-binding protein Polyethylene Glycols Ubiquitin Structural Biology Humans TSG101 Molecular replacement Amino Acid Sequence Peptide sequence chemistry.chemical_classification Endosomal Sorting Complexes Required for Transport biology Chemistry Rational design Water General Medicine Peptide Fragments Recombinant Proteins Protein Structure Tertiary DNA-Binding Proteins Ammonium Sulfate biology.protein Crystallization Hydrophobic and Hydrophilic Interactions Transcription Factors |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 62:458-464 |
| ISSN: | 0907-4449 |
| Popis: | The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition. |
| Databáze: | OpenAIRE |
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