3lms
Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI.Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI.
Template:ABSTRACT PUBMED 20088943
FunctionFunction
[CBPB2_HUMAN] Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.[1]
About this StructureAbout this Structure
3lms is a 2 chain structure with sequence from Homo sapiens and Rhipicephalus bursa. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Sanglas L, Arolas JL, Valnickova Z, Aviles FX, Enghild JJ, Gomis-Ruth FX. Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost. 2010 May;8(5):1056-65. Epub 2010 Jan 17. PMID:20088943 doi:10.1111/j.1538-7836.2010.03740.x
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OCACategories:
- Carboxypeptidase U
- Homo sapiens
- Rhipicephalus bursa
- Arolas, J L.
- Aviles, F X.
- Enghild, J J.
- Gomis-Ruth, F X.
- Sanglas, L.
- Valnickova, Z.
- Alpha-beta-hydrolase
- Blood coagulation
- Carboxypeptidase
- Cogaulation
- Disulfide bond
- Fibrinolysis
- Funnelin
- Glycoprotein
- Hydrolase
- Hydrolase-hydrolase inhibitor complex
- Metal-binding
- Metalloenzyme inhibitor
- Metallopeptidase
- Metalloprotease
- Metalloprotease inhibitor
- Protease
- Secreted
- Zymogen