التفاصيل البيبلوغرافية
| العنوان: |
Structural understanding of stabilization patterns in engineered bispecific Ig-like antibody molecules |
| المؤلفون: |
Guohui Li, Jacob L. Jordan, Karl J. M. Hanf, Janine Hall, Xiufeng Wu, Joseph Arndt, Flora Huang, Deping Wang, Stephen Demarest, Alexey Lugovskoy, Scott Glaser, Erik J. Fernandez, Brian Robert Miller |
| المصدر: |
Proteins: Structure, Function, and Bioinformatics. 77:832-841 |
| بيانات النشر: |
Wiley, 2009. |
| سنة النشر: |
2009 |
| مصطلحات موضوعية: |
Antibody Stabilization, biology, Antigen, Structural Biology, Stereochemistry, Chemistry, biology.protein, Biophysics, Molecule, Antibody, Ligand (biochemistry), Molecular Biology, Biochemistry |
| الوصف: |
Bispecific immunoglobulin-like antibodies capable of engaging multiple antigens represent a promising new class of therapeutic agents. Engineering of these molecules requires optimization of the molecular properties of one of the domain components. Here, we present a detailed crystallographic and computational characterization of the stabilization patterns in the lymphotoxin-beta receptor (LTβR) binding Fv domain of an anti-LTβR/anti-TNF-related apoptosis inducing ligand receptor-2 (TRAIL-R2) bispecific immunoglobulin-like antibody. We further describe a new hierarchical structure-guided approach toward engineering of antibody-like molecules to enhance their thermal and chemical stability. Proteins 2009. © 2009 Wiley-Liss, Inc. |
| تدمد: |
0887-3585 |
| URL الوصول: |
https://explore.openaire.eu/search/publication?articleId=doi_________::05f4a70d2b181a06e14de3d18f34c311
https://doi.org/10.1002/prot.22502 |
| حقوق: |
CLOSED |
| رقم الأكسشن: |
edsair.doi...........05f4a70d2b181a06e14de3d18f34c311 |
| قاعدة البيانات: |
OpenAIRE |
