Therapeutic target-site variability in α(1)-antitrypsin characterized at high resolution

The intrinsic propensity of α(1)-antitrypsin to undergo conformational transitions from its metastable native state to hyperstable forms provides a motive force for its antiprotease function. However, aberrant conformational change can also occur via an intermolecular linkage that results in polymer...

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Detalles Bibliográficos
Autores principales: Patschull, Anathe O. M., Segu, Lakshmi, Nyon, Mun Peak, Lomas, David A., Nobeli, Irene, Barrett, Tracey E., Gooptu, Bibek
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2011
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3232123/
https://www.ncbi.nlm.nih.gov/pubmed/22139150
http://dx.doi.org/10.1107/S1744309111040267

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3232123/
https://www.ncbi.nlm.nih.gov/pubmed/22139150
http://dx.doi.org/10.1107/S1744309111040267

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