Data Set of Publication Replacement of a single residue in an antibody abolishes cognate antigen binding, as predicted by theoretical methods

Name: Data Set of Publication Replacement of a single residue in an antibody abolishes cognate antigen binding, as predicted by theoretical methods
Published: 2025
Keywords: 570 Life sciences

URN to cite this document:: urn:nbn:de:bvb:355-epub-779101
DOI to cite this document:: 10.5283/epub.77910

Rudack, Till

; Scherlo, Marvin

	License: Creative Commons Attribution 4.0 Plain Text - Data (26MB)
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	License: Creative Commons Attribution 4.0 Plain Text - Data (26MB)
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	License: Creative Commons Attribution 4.0 Plain Text - Data (1kB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (1kB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (1kB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (26MB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (21MB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (21MB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (21MB)
	License: Creative Commons Attribution 4.0 Plain Text - Data (1kB)
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	License: Creative Commons Attribution 4.0 Plain Text - Data (21MB)

Date of publication of this fulltext: 08 Oct 2025 07:24

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Details

Item type:	Dataset
Open Access Type:	Primary Publication
Date:	7 October 2025
Institutions:	Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Till Rudack
Dewey Decimal Classification:	500 Science > 570 Life sciences
Status:	Submitted
Refereed:	No, this version has not been refereed yet (as with preprints)
Created at the University of Regensburg:	Yes
Item ID:	77910

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Abstract

Data archive for the publication: Structural insights into the interaction between antibodies and antigens at the atomic level are pivotal for understanding the molecular mechanisms of antigen binding. Despite the availability of structural models generated by recent artificial intelligence advancements, computational predictions require experimental validation to confirm their accuracy. Here, ...