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7VOO

Induced alpha-2-macroglobulin monomer

Summary for 7VOO
Entry DOI10.2210/pdb7voo/pdb
EMDB information32052
DescriptorAlpha-2-macroglobulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsprotease inhibitor, blood clotting
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight147766.67
Authors
Huang, X.,Wang, Y.,Ping, Z. (deposition date: 2021-10-14, release date: 2022-10-19, Last modification date: 2024-11-06)
Primary citationHuang, X.,Wang, Y.,Yu, C.,Zhang, H.,Ru, Q.,Li, X.,Song, K.,Zhou, M.,Zhu, P.
Cryo-EM structures reveal the dynamic transformation of human alpha-2-macroglobulin working as a protease inhibitor.
Sci China Life Sci, 65:2491-2504, 2022
Cited by
PubMed Abstract: Human alpha-2-macroglobulin is a well-known inhibitor of a broad spectrum of proteases and plays important roles in immunity, inflammation, and infections. Here, we report the cryo-EM structures of human alpha-2-macroglobulin in its native state, induced state transformed by its authentic substrate, human trypsin, and serial intermediate states between the native and fully induced states. These structures exhibit distinct conformations, which reveal the dynamic transformation of alpha-2-macro-globulin that acts as a protease inhibitor. The results shed light on the molecular mechanism of alpha-2-macroglobulin in entrapping substrates.
PubMed: 35781771
DOI: 10.1007/s11427-022-2139-2
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

227111

数据于2024-11-06公开中

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