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Glycoprotein Crystal based Glycosylation Site Analysis Service

Beyond the Sugar Coat: Unlocking New Drug Targets with Advanced Glycosylation Analysis

Are you currently facing long drug development cycles, difficulty in identifying novel protein targets, and challenges in engineering effective biologics? Our One-Stop Glycan Crystal & Glycoprotein Crystal Analysis Services help you accelerate drug discovery, obtain high-quality structural data, and develop highly specific therapeutics through advanced structural biology and innovative bioinformatics. At Creative Biolabs, our Glycoprotein Crystal Analysis Services provide more than just a crystal structure, which offers a high-resolution map of your protein's functional landscape. By precisely locating and analyzing every glycan, we uncover critical insights into molecular functions and protein-protein interactions. We provide a clear understanding of how glycosylation dictates your protein's folding, stability, and interaction with other molecules, giving you the knowledge needed for rational drug design and targeted therapeutic development. Our service is designed to reveal novel binding interfaces and guide the engineering of more potent and specific antibodies and vaccines.

Crystal structure of MAG protein. (OA Literature)Fig.1 Crystal structure of myelin-associated glycoprotein.1

Discover the untapped potential of your protein targets - Request a Consultation

Glycosylation is a critical post-translational modification that dictates the structure and function of proteins. Our Glycoprotein Crystal-based Glycosylation Site Analysis Service leverages high-resolution structural biology to precisely map these modifications, providing unprecedented insights into their functional roles. We move beyond simple sequence-based prediction to offer a detailed, atomic-level understanding of how glycans influence molecular interactions, stability, and biological activity, a crucial step for rational drug design and effective therapeutic development. The glycoprotein crystal-based glycosylation site analysis service is a streamlined, methodical process designed to deliver actionable structural intelligence. Our team collaborates closely with your scientists at every stage to ensure the final deliverables are perfectly aligned with your project goals. We transform complex structural data into clear, strategic insights that inform your next steps.

Project Assessment

We begin with a collaborative discussion to define your project objectives, evaluate your starting materials, and design a custom service plan. The expected outcome is a clearly defined scope of work and a project timeline.

Sample Preparation & Crystallization Optimization

Upon receiving your protein, we perform rigorous quality control checks. Our experts then use an extensive array of high-throughput screens and specialized techniques, such as co-crystallization with stabilizing ligands, to identify and optimize conditions for high-quality, diffraction-ready crystals.

X-ray Data Collection

To achieve the resolution necessary to resolve intricate glycan chains, we collect high-quality X-ray diffraction data at a powerful synchrotron facility. This is a critical step that ensures the precision of the final structural model.

Structural Determination & Modeling

Our expert structural biologists process the diffraction data and determine the three-dimensional structure of your glycoprotein. They meticulously model the protein backbone and side chains, followed by the careful placement and refinement of each glycan.

Comprehensive Glycosylation Site Analysis

This is the core of our offering. We meticulously analyze the electron density maps to locate and model the position of each N-linked and O-linked glycan. Our analysis goes beyond a simple list of sites. We investigate:

  • Glycan occupancy: The degree to which each site is glycosylated.
  • Glycan conformation: The specific folding and orientation of the sugar chains.
  • Functional implications: How a specific glycan is involved in stabilizing the protein, interacting with a receptor, or shielding a key epitope.

Technical Platforms

The core of the glycosylation site analysis service based on glycoprotein crystals lies in the organic combination of X-ray crystallography and MS to form a complementary analytical strategy. Our service is powered by state-of-the-art platforms and methods, including:

Advanced analytics platform. (Creative Biolabs Original)

Necessity and Challenges of Analysis

It is imperative to provide a glycoprotein crystal-based glycosylation site analysis service because glycosylation is far from a random decoration. The scientific literature demonstrates its precise and critical roles:

Regulatory function

Glycans can act as molecular switches that activate or inhibit protein function. For example, a glycan on myelin-associated glycoprotein (MAG) acts as a "steric regulator," preventing premature dimerization, while a glycan on a viral protein can be a "regulatory brake," weakening an interaction to ensure it is finely tuned for its biological purpose.

Targeting and architecture

Some proteins, like human β2-glycoprotein I (β2GPI), utilize distinct, non-glycosylated domains for their primary functions, even when other areas are heavily glycosylated for structural purposes. Identifying these glycan-free hotspots is critical for developing targeted therapies.

Immune evasion

Viruses can heavily glycosylate their surface proteins to cloak key functional regions from the host's immune system. Understanding this structure is essential for designing antibodies and vaccines that can successfully bypass this defense.

The glycoprotein crystal-based glycosylation site analysis service stands at the intersection of biochemistry, structural biology, and computational analysis. Its goal is to overcome a significant challenge in the field: the inherent flexibility and heterogeneity of glycan chains, which often make them difficult to resolve in crystal structures. Traditional methods, such as mass spectrometry (MS), provide excellent data on the composition of glycans but lack the three-dimensional structural context required to understand their functional roles. Furthermore, obtaining high-quality crystals of heavily glycosylated proteins remains a technical bottleneck, requiring specialized expertise.

Published Data

The researchers determined crystal structures of myelin-associated glycoprotein (MAG) full ectodomain, revealing an extended, collinear conformation of its five immunoglobulin (Ig) domains. A key discovery was the identification of a homodimeric arrangement involving the membrane-proximal Ig4 and Ig5 domains. This dimerization is supported by a large, hydrophobic interface. Using structure-guided mutations and biophysical assays like small-angle X-ray scattering (SAXS) and analytical ultracentrifugation (AUC), the authors validated this dimerization interface. They showed that the I473E mutation disrupts dimerization, causing the protein to remain a monomer, while the N406Q mutation enhances it. The team found that N-linked glycosylation at asparagine 406 plays a regulatory role in dimerization. As depicted in the Figure, the glycan at this site sterically clashes with the symmetry partner in the dimer, suggesting that its presence inhibits dimerization. By mutating N406 to glutamine to prevent this glycosylation, the researchers created a MAG variant with enhanced dimerization properties. The SAXS data presented in the Figure further confirmed these observations, showing that the glycosylated wild-type MAG exists in a monomer-dimer equilibrium, while the N406Q mutant strongly favors the dimeric state. This suggests that the presence of the glycan acts as a switch, modulating MAG's ability to form dimers and consequently its functions.

Dimerization and verification results of MAG crystals. (OA Literature)Fig.2 Dimerization of MAG protein crystals and its verification.1

FAQs

What kind of glycoproteins are suitable for your analysis service?

We can analyze a wide range of glycoproteins, including viral envelope proteins, cell surface receptors, and therapeutic antibodies. The primary requirement is a highly pure and stable protein sample. If you have a particularly challenging protein, our team can work with you to optimize it for crystallization and analysis.

How does your service differ from MS-based glycoproteomics?

While MS provides excellent data on the composition and site-location of glycans, our service provides atomic-resolution structural context. We can show you exactly how a glycan is oriented in 3D space, how it interacts with neighboring residues, and how it impacts protein folding - insights that are impossible to obtain with mass spec alone.

What if my protein is difficult to crystallize?

We have extensive expertise in crystallizing challenging proteins. Our methods include high-throughput screening, co-crystallization with stabilizing molecules, and strategic protein engineering to remove flexible domains. Many projects that fail to crystallize elsewhere find success with us.

Customer Review

Significant Improvement in Stability
"Using Creative Biolabs' glycoprotein crystal-based glycosylation site analysis service in our research has significantly improved the stability of our recombinant protein. We discovered that a specific glycan was causing conformational instability, and our subsequent engineering efforts based on Creative Biolabs' recommendations yielded a dramatically more stable and manufacturable therapeutic candidate."- J***n, Scientist.

Unlocking Novel Targets
"We were at a dead end in our search for new therapeutic targets for an autoimmune disease. Creative Biolabs' analysis of a key plasma protein revealed a previously uncharacterized, non-glycosylated domain critical for its function. This opened up an entirely new avenue for our research and has given us a significant lead in the market."- M***a, Project manager.

How to Contact Us

Creative Biolabs is committed to providing world-class scientific services to help you reach your goals. Our team of experts is ready to discuss your specific project needs and provide a customized solution. In addition to the glycosylation site analysis service, we provide various glycoprotein crystal analysis services, including Structural Analysis, Glycosylation Type Analysis, and Glycoprotein & Carbohydrate Binding Analysis services. Please contact us for more information.

Reference

  1. Pronker, Matti F., et al. "Structural basis of myelin-associated glycoprotein adhesion and signalling." Nature Communications 7.1 (2016): 13584. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.1038/ncomms13584
For Research Use Only.

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