Comparison of structures indicated that the selectivity of interactions between cysteine cathepsins and the p41 fragment is far from being understood and requires further investigation. The p41 fragment has now been shown also to inhibit human cathepsins V, K and F (also, presumably, O) and mouse cathepsin L with Ki values in the low nM range and surprisingly cathepsin S too. These findings suggest that regulation of the proteolytic activity of most of the cysteine cathepsins by the p41 fragment is an important and widespread control mechanism of antigen presentation.
COBISS.SI-ID: 21555495
A database of geometric restraint for refinement of heteromolecules in complexes with macromolecules was derived by statistical analysis of structures of small molecules deposited in Cambridge Crystal Structure Database in an automated manner. With these also geometric restraints of hetero compounds became of comparable quality with those of amino and nucleic acid residues. The data base has a web server access.
COBISS.SI-ID: 22118695
The tertrameric structure of stefin B P79S mutant has exposed the importance of proline isomerization in amyloid fibril formation of stefin B.
COBISS.SI-ID: 20673831
Comparison of inhibition constants between human and mouse cathepsins and stefins revealed that there are differences between the mouse and human proteins involved in intracellular degradation and immune response, indicating a possibility of different degradation pathways. Times cited: 2
COBISS.SI-ID: 20097063
The structure has proven that the double head epoxysuccinyl based inhibitors indeed can bind along the active site cleft as proposed (Turk et al., 1996,Biochemistry 34, 4791-4797). Times cited: 9
COBISS.SI-ID: 18604327