Chymotrypsin Inhibitor
From Proteopedia
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CI inhibition is achieved by the <scene name='43/430100/Cv/3'>insertion of a loop into the serine protease active site</scene>. <ref>PMID:15504027</ref> | CI inhibition is achieved by the <scene name='43/430100/Cv/3'>insertion of a loop into the serine protease active site</scene>. <ref>PMID:15504027</ref> | ||
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| + | == 3D Structures of Chymotrypsin inhibitor == | ||
| + | [[Chymotrypsin inhibitor 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
== 3D Structures of Chymotrypsin Inhibitor == | == 3D Structures of Chymotrypsin Inhibitor == | ||
Revision as of 08:24, 13 May 2019
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3D Structures of Chymotrypsin Inhibitor
Updated on 13-May-2019
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
