Chymotrypsin Inhibitor

From Proteopedia

Revision as of 09:22, 20 October 2017

spinqualitylabelsall models Chymotrypsin Inhibitor 2 (cyan) complex with subtilisin (magenta), PEG, citrate, Ca+2 (green) and Na+ (purple) ions (PDB entry 1to1) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Chymotrypsin Inhibitors (CI) are serine proteinase inhibitors of chymotrypsin. They are classified by numbers: CI-1[1], CI-2[2], CI-3[3]. Subtilisin-chymotrypsin inhibitor inhibits both subtilisin and chymotrypsin. Structural highlights CI inhibition is achieved by the . [4]

3D Structures of Chymotrypsin Inhibitor

Updated on 20-October-2017

References

1. ↑ Huang K, Strynadka NC, Bernard VD, Peanasky RJ, James MN. The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure. 1994 Jul 15;2(7):679-89. PMID:7922044
2. ↑ McPhalen CA, James MN. Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry. 1987 Jan 13;26(1):261-9. PMID:3828302
3. ↑ Ravichandran S, Sen U, Chakrabarti C, Dattagupta JK. Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1814-21. PMID:10531477
4. ↑ Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr. Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex. Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027 doi:http://dx.doi.org/10.1021/bi048797k