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Unveiling interactions between proteolytic enzymes, their inhibitors and protein ligands/substrates by MS-functional proteomics
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

Unveiling interactions between proteolytic enzymes, their inhibitors and protein ligands/substrates by MS-functional proteomics


5th International Conference on Proteomics & Bioinformatics

September 01-03, 2015 Valencia, Spain

Aviles F X, Tanco S, Covaleda G, Tort O, Otero A, Vendrell J and Lorenzo J

Universitat Autonoma de Barcelona, Spain

Posters-Accepted Abstracts: J Proteomics Bioinform

Abstract :

Presently, there is a tendency towards an integrated view of proteolytic enzymes (proteases) and partners in vivo, particularly in the genomics-proteomics-interactomics context. This is also valid for one of their frequent variants like metalloproteases and within them for metallo-carboxypeptidases (MCPs or CPs). The strong growth in the number of MCPs in the last decade has not been paralleled with the understanding of how they act simultaneously or specifically on natural substrates neither on their ligands and inhibitors. The fact that such binders-effectors frequently are of proteic nature, adds further degrees of sophistication to these interactions as well as to the modulation of activities and specificities that they promote. Nowadays we could estimate around 30 the number of variants of such MCPs classified among the M14A, B and C forms and the recently emerged cytosolic forms (CCPs) for the M14D subfamily. Since all of them seem to keep the ├ó┬?┬?canonic├ó┬?┬Ł domain of metallocarboxypeptidases and equivalent recognition sites, it is a real challenge in understanding of their complex relationships, their discriminative interactions with natural substrates (peptidic or proteic, since they are proteases) and with the environmental protein inhibitors. The same happens in the design of drugs through the generation of specific ligands that could control such proteases. MCPs like other proteases share another characteristic interactomics property: They act transiently over protein substrates promoting cleavages which strongly affect conformations and functionalities. How to detect such interactions usually is not an easy task although feasible. Also, the occurrence and role that play in nature numerous protein inhibitors of them usually is poorly known. The talk will focus on cases of recently discovery of such inhibitors and/or ligands-substrates and about strategies of proteomics, interactomics and others followed for its identification and characterization.

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