Explore the Potential with AI-Driven Innovation
This extensive focused library is tailor-made using the latest virtual screening and parameter assessment technology, operated by the Receptor.AI drug discovery platform. This technique is more effective than traditional methods, offering compounds with improved activity, selectivity, and safety.
Our selection of compounds is from a large virtual library of over 60 billion molecules. The production and distribution of these compounds are managed by our partner Reaxense.
Contained in the library are leading modulators, each labelled with 38 ADME-Tox and 32 physicochemical and drug-likeness qualities. In addition, each compound is illustrated with its optimal docking poses, affinity scores, and activity scores, giving a complete picture.
We utilise our cutting-edge, exclusive workflow to develop focused libraries.
Fig. 1. The sreening workflow of Receptor.AI
Our methodology leverages molecular simulations to examine a vast array of proteins, capturing their dynamics in both isolated forms and in complexes with other proteins. Through ensemble virtual screening, we thoroughly account for the protein's conformational mobility, identifying critical binding sites within functional regions and distant allosteric locations. This detailed exploration ensures that we comprehensively assess every possible mechanism of action, with the objective of identifying novel therapeutic targets and lead compounds that span a wide spectrum of biological functions.
Our library stands out due to several important features:
partner
Reaxense
upacc
Q01130
UPID:
SRSF2_HUMAN
Alternative names:
Protein PR264; Splicing component, 35 kDa; Splicing factor SC35; Splicing factor, arginine/serine-rich 2
Alternative UPACC:
Q01130; B3KWD5; B4DN89; H0YG49
Background:
Serine/arginine-rich splicing factor 2 (SRSF2), also known as Protein PR264, Splicing component, 35 kDa, Splicing factor SC35, and Splicing factor, arginine/serine-rich 2, plays a pivotal role in pre-mRNA splicing. It facilitates the earliest ATP-dependent splicing complex formation, interacting with spliceosomal components at both 5'- and 3'-splice sites during spliceosome assembly. SRSF2 is essential for ATP-dependent U1 and U2 snRNPs interactions with pre-mRNA, forming a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. It binds to purine-rich RNA sequences and is crucial for committing beta-globin mRNA to the splicing pathway. Its phosphorylated form is vital for cellular apoptosis in response to cisplatin treatment.
Therapeutic significance:
Understanding the role of Serine/arginine-rich splicing factor 2 could open doors to potential therapeutic strategies.