4A5T

STRUCTURAL BASIS FOR THE CONFORMATIONAL MODULATION

Summary for 4A5T

• Entry DOI: 10.2210/pdb4a5t/pdb
• Related: 1B2I 1BML 1BUI 1CEA 1CEB 1DDJ 1HPJ 1HPK 1I5K 1KI0 1KRN 1L4D 1L4Z 1PK4 1PKR 1PMK 1QRZ 1RJX 2PK4 5HPG
• Descriptor: PLASMINOGEN, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose, CHLORIDE ION (3 entities in total)
• Functional Keywords: hydrolase, multi-domain conformational change
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 89289.97

Authors

Xue, Y.,Bodin, C.,Olsson, K. (deposition date: 2011-10-28, release date: 2012-05-23, Last modification date: 2020-07-29)

Primary citation

Xue, Y.,Bodin, C.,Olsson, K.
Crystal Structure of the Native Plasminogen Reveals an Activation-Resistant Compact Conformation.
J. Thromb. Haemost., 10:1385-, 2012

PubMed Abstract: Plasminogen is the zymogen form of plasmin and the precursor of angiostatin. It has been implicated in a variety of disease states, including thrombosis, bleeding and cancers. The native plasminogen, known as Glu-plasminogen, contains seven domains comprising the N-terminal peptide domain (NTP), five kringle domains (K1-K5) and the C-terminal serine protease domain (SP). Previous studies have established that the lysine binding site (LBS) of the conserved kringle domains plays a crucial role in mediating the regulation of plasminogen function. However, details of the related conformational mechanism are unknown.

PubMed: 22540246
DOI: 10.1111/J.1538-7836.2012.04765.X

Experimental method

X-RAY DIFFRACTION (3.49 Å)