Kallikrein

From Proteopedia

spinqualitylabelsall models Structure of human kallikrein 4 complex with p-aminobenzamidine and Zn+2 ion (grey) (PDB code 2bdh) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights 4 3D Structures of kallikrein Function Kallikrein (KLK) is a serine protease. Plasma KLK releases the peptides bradykinin and kallidin from kininogen and plasmin from plasminogen. Tissue KLK participates in the regulation of blood pressure by activation of bradykinin[1]. KLK1 releases the vasoactive peptide Lys-bradikinin from kininogen. KLK2 is prostate-specific. KLK4 cleaves extracellular matrix proteins. KLK5 and KLK7 regulate cell shedding. KLK6 regulates immune cells survival. KLK8 is involved inproteolytic cascade in the skin. plasma KLK cleaves Arg and Lys in kininogen to release bradykinin. Tissue KLK is expressed throughout the body. Disease Activation of the plasma KLK pathway may contribute to diabetic macular edema[2]. KLK6 is implicated in carcinogenesis, Alzheimer and Parkinson diseases[3]. KLK8 processes papilloma virus fascilitating their entry to host cells[4]. . Structural highlights KLK being a serine protease contains the [5]. Water molecules shown as red spheres. 3D Structures of kallikrein Kallikrein 3D structures

References

1. ↑ Bryant JW, Shariat-Madar Z. Human plasma kallikrein-kinin system: physiological and biochemical parameters. Cardiovasc Hematol Agents Med Chem. 2009 Jul;7(3):234-50. PMID:19689262
2. ↑ Feener EP. Plasma kallikrein and diabetic macular edema. Curr Diab Rep. 2010 Aug;10(4):270-5. doi: 10.1007/s11892-010-0127-1. PMID:20535647 doi:http://dx.doi.org/10.1007/s11892-010-0127-1
3. ↑ Pampalakis G, Sotiropoulou G. Multiple mechanisms underlie the aberrant expression of the human kallikrein 6 gene in breast cancer. Biol Chem. 2006 Jun;387(6):773-82. PMID:16800739 doi:http://dx.doi.org/10.1515/BC.2006.097
4. ↑ Cerqueira C, Samperio Ventayol P, Vogeley C, Schelhaas M. Kallikrein-8 Proteolytically Processes Human Papillomaviruses in the Extracellular Space To Facilitate Entry into Host Cells. J Virol. 2015 Jul;89(14):7038-52. doi: 10.1128/JVI.00234-15. Epub 2015 Apr 29. PMID:25926655 doi:http://dx.doi.org/10.1128/JVI.00234-15
5. ↑ Debela M, Magdolen V, Grimminger V, Sommerhoff C, Messerschmidt A, Huber R, Friedrich R, Bode W, Goettig P. Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site. J Mol Biol. 2006 Oct 6;362(5):1094-107. Epub 2006 Aug 3. PMID:16950394 doi:10.1016/j.jmb.2006.08.003