Framework-Mediated Glycan Binding by IGHV4-34 Antibodies: A Structural Analysis

A 752 KB document authored by David B. Langley and last updated on March 17, 2026. It presents structural insights into the binding mechanism of IGHV4-34 antibodies to self and foreign glycans, focusing on the role of a hydrophobic patch in framework region 1. The analysis connects findings from HIV envelope glycoprotein studies to autoimmune conditions like cold agglutinin disease.

Use Cases

• Study antibody framework-mediated antigen binding based on the described FR1 hydrophobic patch.
• Analyze structural similarities between HIV high mannose glycans and self-antigen LacNAc polymers.
• Investigate the mechanistic role of germline-encoded residues in autoantibody function.
• Model non-CDR (complementarity-determining region) binding modes for carbohydrate antigens.

Strengths

• Document is under a permissive CC-BY-4.0 license.
• Author is explicitly named (David B. Langley).
• Last update date is precisely recorded (2026-03-17).

Limitations

• The dataset is a 752 KB DOCX file, indicating a very small textual document rather than a large-scale dataset.
• Row count and column-level documentation are unknown, limiting suitability assessment.
• The description is highly specific to a niche biological mechanism; generalizability is limited.

Provenance

Source

figshare

Collection Method

Likely a research document authored by the named individual.

Time Range

Publication date not specified; last updated March 2026.

Freshness

Last updated 2026-03-17 13:07:01.

Geography

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