| 1. |
- Axblom, C, et al.
(författare)
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Structure of phage fr capsids with a deletion in the FG loop: Implications for viral assembly
- 1998
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Ingår i: VIROLOGY. - : ACADEMIC PRESS INC. - 0042-6822. ; 249:1, s. 80-88
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- The loop between beta-strands F and G in the coat protein of small RNA bacteriophages forms the interactions at the fivefold and threefold (quasi-sixfold) icosahedral axes. In many cases, mutations in this region renders the coat protein unable to form ca
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| 2. |
- Golmohammadi, R, et al.
(författare)
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The crystal structure of bacteriophage Q beta at 3.5 angstrom resolution
- 1996
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Ingår i: STRUCTURE. - : CURRENT BIOLOGY LTD. - 0969-2126. ; 4:5, s. 543-554
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- Background: The capsid protein subunits of small RNA bacteriophages form a T=3 particle upon assembly and RNA encapsidation. Dimers of the capsid protein repress translation of the replicase gene product by binding to the ribosome binding site and this in
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| 5. |
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| 6. |
- Tars, K, et al.
(författare)
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Structure determination of bacteriophage PP7 from Pseudomonas aeroginosa: from poor data to a good map
- 2000
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Ingår i: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. - : MUNKSGAARD INT PUBL LTD. - 0907-4449. ; 56, s. 398-405
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Tidskriftsartikel (refereegranskat)abstract
- The structure of bacteriophage PP7 from Pseudomomas aeruginosa was determined to 3.7 Angstrom resolution. Triclinic crystals of three forms were obtained, diffracting to between 4.5 and 3.4 Angstrom resolution. The quality of the crystals was exceptionall
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| 7. |
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| 8. |
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| 9. |
- van, den Worm SHE, et al.
(författare)
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Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments
- 1998
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Ingår i: NUCLEIC ACIDS RESEARCH. - : OXFORD UNIV PRESS. - 0305-1048. ; 26:5, s. 1345-1351
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Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
- In MS2 assembly of phage particles results from an interaction between a coat protein dimer and a stem-loop of the RNA genome (the operator hairpin), Amino acid residues Thr45, which is universally conserved among the small RNA phages, and Thr59 are part
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| 10. |
- Andersson, H.O., et al.
(författare)
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Optimization of P1-P3 groups in symmetric and asymmetric HIV-1 protease inhibitors
- 2003
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Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 270:8, s. 1746-1758
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Tidskriftsartikel (refereegranskat)abstract
- HIV-1 protease is an important target for treatment of AIDS, and efficient drugs have been developed. However, the resistance and negative side effects of the current drugs has necessitated the development of new compounds with different binding patterns. In this study, nine C-terminally duplicated HIV-1 protease inhibitors were cocrystallised with the enzyme, the crystal structures analysed at 1.8-2.3 Å resolution, and the inhibitory activity of the compounds characterized in order to evaluate the effects of the individual modifications. These compounds comprise two central hydroxy groups that mimic the geminal hydroxy groups of a cleavage-reaction intermediate. One of the hydroxy groups is located between the d-oxygen atoms of the two catalytic aspartic acid residues, and the other in the gauche position relative to the first. The asymmetric binding of the two central inhibitory hydroxyls induced a small deviation from exact C2 symmetry in the whole enzyme-inhibitor complex. The study shows that the protease molecule could accommodate its structure to different sizes of the P2/P2' groups. The structural alterations were, however, relatively conservative and limited. The binding capacity of the S3/S3' sites was exploited by elongation of the compounds with groups in the P3/P3' positions or by extension of the P1/P1' groups. Furthermore, water molecules were shown to be important binding links between the protease and the inhibitors. This study produced a number of inhibitors with Ki values in the 100 picomolar range.
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