Cited by 5Peptidase Inhibition and AnalysisMonoclonal and Polyclonal Antibodies ResearchEnzyme Structure and Function

Cryo-electron microscopy reveals a single domain antibody with a unique binding epitope on fibroblast activation protein alpha

Open access
Xu, Zhen, Sinha, Akesh, Pandya, Darpan N., Schnicker, Nicholas J., Wadas, Thaddeus J.·2025·RSC Chemical Biology

Published version of a preprint

Abstract

The single domain antibody, I3, interacts with fibroblast activation protein alpha through its CDR3 loop and FR2 region to bind a unique and previously undisclosed epitope that is distinct from the protease's active site.

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Integrity signals

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Crossref · 10.1039/d4cb00267a

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2 of 2 references verified0 citation errors · 0 not checkable

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Authors
Xu, Z., Sinha, A., Pandya, D. N., Schnicker, N. J., & Wadas, T. J.
Affiliations
University of Iowa (US)
Corresponding author
  • Schnicker, Nicholas J.
  • Wadas, Thaddeus J.
Venue
RSC Chemical Biology
Published
2025
Volume
6
Issue
5
Pages
780-787
ISSN
2633-0679 (ISSN-L)
OpenAlex
W4407219915
Cited by
5
References
2
Citations by year
2026: 3 · 2025: 2
FWCI
2.07
Type
journal article
Language
en
Open access
Locations
  • RSC Chemical Biology (publishedVersion, cc-by-nc)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by-nc)
  • PubMed (publishedVersion)
  • PubMed Central (submittedVersion, cc-by-nc)
Funders
  • Congressionally Directed Medical Research Programs (W81XWH-19-1-0046)
  • Division of Cancer Prevention, National Cancer Institute (P30CA086862, R21-CA219899, R21-CA227709)
Topics
  • Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
  • Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
fibroblast activation protein, nanobodies, antibody-antigen complex structure, binding epitope, serine protease, CDR3, protein dimer

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