AI-ACCELERATED DRUG DISCOVERY

Focused On-demand Library for Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1

Available from Reaxense
Predicted by Alphafold

Focused On-demand Libraries - Reaxense Collaboration

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.

From a virtual chemical space containing more than 60 billion molecules, we precisely choose certain compounds. Our collaborator, Reaxense, aids in their synthesis and provision.

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.

Our high-tech, dedicated method is applied to construct targeted libraries.

 Fig. 1. The sreening workflow of Receptor.AI

Our strategy employs molecular simulations to explore an extensive range of proteins, capturing their dynamics both individually and within complexes with other proteins. Through ensemble virtual screening, we address proteins' conformational mobility, uncovering key binding sites at both functional regions and remote allosteric locations. This comprehensive investigation ensures a thorough assessment of all potential mechanisms of action, with the goal of discovering innovative therapeutic targets and lead molecules across across diverse biological functions.

Our library distinguishes itself through several key aspects:

  • The Receptor.AI platform integrates all available data about the target protein, including past experiments, literature data, known ligands, structural information and more. This consolidated approach maximises the probability of prioritising highly relevant compounds.
  • The platform uses sophisticated molecular simulations to identify possible binding sites so that the compounds in the focused library are suitable for discovering allosteric inhibitors and the binders for cryptic pockets.
  • The platform integrates over 50 highly customisable AI models, which are thoroughly tested and validated on a multitude of commercial drug discovery programs and research projects. It is designed to be efficient, reliable and accurate. All this power is utilised when producing the focused libraries.
  • In addition to producing the focused libraries, Receptor.AI provides services and end-to-end solutions at every stage of preclinical drug discovery. The pricing model is success-based, which reduces your risks and leverages the mutual benefits of the project's success.

partner

Reaxense

upacc

P04843

UPID:

RPN1_HUMAN

Alternative names:

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit; Ribophorin I; Ribophorin-1

Alternative UPACC:

P04843; B2R5Z0; D3DNB6; Q68DT1

Background:

Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1, also known as Ribophorin I or Ribophorin-1, plays a crucial role in protein N-glycosylation. This process involves the transfer of a specific glycan from dolichol-pyrophosphate to an asparagine residue within nascent polypeptide chains. It occurs cotranslationally and is essential for protein folding and stability. The protein is part of the oligosaccharyl transferase (OST) complex, which associates with the Sec61 complex at the ER translocon, facilitating protein translocation across the endoplasmic reticulum.

Therapeutic significance:

Understanding the role of Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 could open doors to potential therapeutic strategies.

Looking for more information on this library or underlying technology? Fill out the form below and we'll be in touch with all the details you need.
Thank you! Your submission has been received!
Oops! Something went wrong while submitting the form.