SHREC2020 track:Multi-domain protein shape retrieval challenge

Proteins are natural modular objects usually composed of several domains, each domain bearing a specific function that is mediated through its surface, which is accessible to vicinal molecules. This draws attention to an understudied characteristic of protein structures: surface, that is mostly unexploited by protein structure comparison methods. In the present work, we evaluated the performance of six shape comparison methods, among which three are based on machine learning, to distinguish between 588 multi-domain proteins and to recreate the evolutionary relationships at the proteinand species levels of the SCOPe database. The six groups that participated in the challenge submitted a total of 15 sets of results. We observed that the performance of all the methods significantly decreases at the species level, suggesting that shape-only protein comparison is challenging for closely related proteins. Even if the dataset is limited in size (only 588 proteins are considered whereas more than 160,000 protein structures are experimentally solved), we think that this work provides useful insights into the current shape comparison methods performance, and highlights possible limitations to large-scale applications due to the computational cost

Surface-based protein domains retrieval methods from a SHREC2021 challenge

publication dans une revue suite à la communication hal-03467479 (SHREC 2021: surface-based protein domains retrieval)International audienceProteins are essential to nearly all cellular mechanism and the effectors of the cells activities. As such, they often interact through their surface with other proteins or other cellular ligands such as ions or organic molecules. The evolution generates plenty of different proteins, with unique abilities, but also proteins with related functions hence similar 3D surface properties (shape, physico-chemical properties, …). The protein surfaces are therefore of primary importance for their activity. In the present work, we assess the ability of different methods to detect such similarities based on the geometry of the protein surfaces (described as 3D meshes), using either their shape only, or their shape and the electrostatic potential (a biologically relevant property of proteins surface). Five different groups participated in this contest using the shape-only dataset, and one group extended its pre-existing method to handle the electrostatic potential. Our comparative study reveals both the ability of the methods to detect related proteins and their difficulties to distinguish between highly related proteins. Our study allows also to analyze the putative influence of electrostatic information in addition to the one of protein shapes alone. Finally, the discussion permits to expose the results with respect to ones obtained in the previous contests for the extended method. The source codes of each presented method have been made available online

SHREC 2021: surface-based protein domains retrieval

Oral. 3DOR is the dedicated workshop series for methods, applications and benchmark-based evaluation of 3D object retrieval, classification, and similarity-based object processing. The workshop also includes the 2021 edition of the 3D Shape Retrieval Challenge (SHREC). Accepted full papers will be published in Computers & Graphics Journal (Elsevier), and accepted short papers will appear in the Eurographics Digital Library.International audienceProteins are essential to nearly all cellular mechanism, and often interact through their surface with other cell molecules, such as proteins and ligands. The evolution generates plenty of different proteins, with unique abilities, but also proteins with related functions hence surface, which is therefore of primary importance for their activity. In the present work, we assess the ability of five methods to retrieve similar protein surfaces, using either their shape only (3D meshes), or their shape and the electrostatic potential at their surface, an important surface property. Five different groups participated in this challenge using the shape only, and one group extended its pre-existing algorithm to handle the electrostatic potential. The results reveal both the ability of the methods to detect related proteins and their difficulties to distinguish between topologically related proteins