1JBU

Coagulation Factor VII Zymogen (EGF2/Protease) in Complex with Inhibitory Exosite Peptide A-183

Summary for 1JBU

• Entry DOI: 10.2210/pdb1jbu/pdb
• Related: 1CVW 1DAN 1DVA 1FAK 1QFK
• Descriptor: COAGULATION FACTOR VII, Peptide exosite inhibitor A-183, SULFATE ION, ... (6 entities in total)
• Functional Keywords: shifted registration, beta-strands, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P08709 P08709
• Total number of polymer chains: 3
• Total formula weight: 37191.41

Authors

Eigenbrot, C.,Kirchhofer, D.,Dennis, M.S.,Santell, L.,Lazarus, R.A.,Stamos, J.,Ultsch, M.H. (deposition date: 2001-06-06, release date: 2001-07-11, Last modification date: 2024-10-30)

Primary citation

Eigenbrot, C.,Kirchhofer, D.,Dennis, M.S.,Santell, L.,Lazarus, R.A.,Stamos, J.,Ultsch, M.H.
The factor VII zymogen structure reveals reregistration of beta strands during activation.
Structure, 9:627-636, 2001

PubMed Abstract: Coagulation factor VIIa (FVIIa) contains a Trypsin-like serine protease domain and initiates the cascade of proteolytic events leading to Thrombin activation and blood clot formation. Vascular injury allows formation of the complex between circulating FVIIa and its cell surface bound obligate cofactor, Tissue Factor (TF). Circulating FVIIa is nominally activated but retains zymogen-like character and requires TF in order to complete the zymogen-to-enzyme transition. The manner in which TF exerts this effect is unclear. The structure of TF/FVIIa is known. Knowledge of the zymogen structure is helpful for understanding the activation transition in this system.

PubMed: 11470437
DOI: 10.1016/S0969-2126(01)00624-4

Experimental method

X-RAY DIFFRACTION (2 Å)