1.

Renko M., Sabotič J., Mihelič M., Brzin J., Kos J. and Turk D. (2010): Versatile loops in mycocypins inhibit three protease families.

Mycocypins are cysteine protease inhibitors isolated from the mushrooms Clitocybe nebularis and Macrolepiota procera. The crystal structures of the complex of clitocypin with the papain-like cysteine protease cathepsin V and of macrocypin and clitocypin alone have revealed yet another motif of binding to papain like-cysteine proteases. The binding loops present a versatile surface with the potential to bind to additional classes of proteases. When appropriately engineered, they could provide the basis for possible exploitation in crop protection.

COBISS.SI-ID: 23263527

2.

Stefin A displaces the occluding loop of cathepsin B only by as much as required to bind to the active site cleft.

Cathepsin B (EC 3.4.22.1) is important for intracellular protein degradation and is involved in a number of pathological processes. To clarify the structural properties of the occluding loop upon the binding of stefins, we determined the crystal structure of the complex between wild-type human stefin A and wild-type human cathepsin B. A comparison of the structure of the unliganded cathepsin B with the structure of the proenzyme, its complexes with chagasin and stefin A shows that the magnitude of the shift of the occluding loop is related to the size of the binding region.

COBISS.SI-ID: 24643111

3.

Amyloid fibril formation by human stefins: Structure, mechanism & putative functions.

This review summaries the studies of amyloid fibril formation and pathway intermediates using the human stefins A an B as a working models. These studies provide insight into oligomeric structures as domain swapped dimers and tetrames, their dependance on proline isomerization and energetics of steps between the intermediates. The use of cell models has shown toxicity of prefibrillar oligomers on cells via interactions one acidic phospholipids.

COBISS.SI-ID: 23646247

4.

Single-chain Fv antibody fragments retain binding properties of the monoclonal antibody raised against peptide P1 of the human prion protein.

recombinant single chain antibody fragment (scFv) that specifically recognizes the pathological prion isoform was prepared. It is based on the V5B2 monoclonal antibody directed against a peptide from the C-terminus of the prion protein. We found out that the two opposing orientations of the light and heavy immunoglobulin domains differ in their immunological activity and that the recombinant scFv retained the specificity of the parent antibody. Recombinant scFvs are suitable for diagnostics and can be easily prepared in bacterial cells.

COBISS.SI-ID: 30601477

5.

Parallel approaches to structural biology of immune response - bottlenecks in the production of challenging human proteins

We have verified suitability of expression systems (bacteria, yeast, insect and mammalian cells) for production of human and mouse lysosomal proteins and found out that only insect and mammalian cells are suitable for their expression.

COBISS.SI-ID: 24159015