Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site‐Specific Conjugation. Issue 45 (14th September 2015)

• Record Type: Journal Article
• Authors: Siegmund, Vanessa; Schmelz, Stefan; Dickgiesser, Stephan; Beck, Jan; Ebenig, Aileen; Fittler, Heiko; Frauendorf, Holm; Piater, Birgit; Betz, Ulrich A. K.; Avrutina, Olga; Scrima, Andrea; Fuchsbauer, Hans‐Lothar; Kolmar, Harald
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 45(2015)
• Page Start: 13420
• Page End: 13424
• Publication Date: 2015-09-14
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201504851
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Based on the crystal structure of a natural protein substrate for microbial transglutaminase, an enzyme that catalyzes protein crosslinking, a recognition motif for site‐specific conjugation was rationally designed. Conformationally locked by an intramolecular disulfide bond, this structural mimic of a native conjugation site ensured efficient conjugation of a reporter cargo to the therapeutic monoclonal antibody cetuximab without erosion of its binding properties.</p> </abstract>