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Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
It is suggested that the exclusion domain originates from a metallo‐protease inhibitor, characterized in people suffering from Haim–Munk and Papillon–Lefevre syndromes, suggests how they disrupt the fold and function of the enzyme. Expand
Inositol hexakisphosphate kinase products contain diphosphate and triphosphate groups.
It is reported that IP6K synthesizes both pyrophosphate (diphospho) as well as triphospho groups on the inositol ring, defined by the architecture of IP 6K's active site. Expand
Revised Definition of Substrate Binding Sites of Papain-Like Cysteine Proteases
A review of kinetic and structural data has enabled us to reconsider the definition of substrate binding sites in papain-like cysteine proteases. Only three substrate binding sites, S2, S1 and S1',… Expand
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
- G. Guncar, M. Podobnik, J. Pungercar, B. Strukelj, V. Turk, D. Turk
- Medicine, Chemistry
- 15 January 1998
The crystal structure of cathepsin H reveals that themini-chain has a definitive role in substrate recognition and that carbohydrate residues attached to the body of the enzyme are involved in positioning the mini-chain in the active-site cleft. Expand
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.
- Saša Jenko, I. Dolenc, G. Guncar, A. Doberšek, M. Podobnik, D. Turk
- Chemistry, Medicine
- Journal of molecular biology
- 21 February 2003
Carboxymethylation of papain seems to have prevented the formation of the genuine binding geometry between a papain-like enzyme and a cystatin-type inhibitor as the authors observe it in the structure presented here. Expand
Structural basis for the multitasking nature of the potato virus Y coat protein
The near-atomic structure of PVY’s flexuous virions is determined, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. Expand
Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.
The structure confirms the role of residues His 110 and His 111 as the receptors of a peptidic substrate C-terminal carboxylic group and suggests that an epoxysuccinyl fragment can be used to extend binding into primed and nonprimed substrate binding sites of a papain-like cysteine protease. Expand
Plasticity of Listeriolysin O Pores and its Regulation by pH and Unique Histidine
This work reports that the assembly of LLO pores is rapid and efficient irrespective of pH, and indicates significant plasticity of large β-barrel pores, controlled by environmental cues like pH. Expand
Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
Mutagenic analysis and atomic force microscopy imaging suggest a mechanism for pore assembly for lysenin, which is relevant to the understanding of pore formation by other aerolysin-like pore-forming toxins, which often represent crucial virulence factors in bacteria. Expand
Structural analysis of the inactive state of the Escherichia coli DNA polymerase clamp-loader complex.
- S. Kazmirski, M. Podobnik, Tanya F. Weitze, M. O’Donnell, J. Kuriyan
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 30 November 2004
The results, along with data from isothermal titration calorimetry, molecular dynamics simulations, and comparison with the RFC structure, suggest that the more open form of the E. coli clamp loader corresponds to a stable inactive state of the clamp loader in which the ATPase domains are prevented from engaging the clamp in the highly cooperative manner seen in the fully ATP-loaded RFC-clamp structure. Expand