Chymotrypsin Inhibitor

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(New page: Crystal Structure of Chymotrypsin Inhibitor 4wbc {{STRUCTURE_4wbc| PDB=4wbc | SIZE=300| SCENE= |right|CAPTION=Chymotrypsin Inhibitor 4wbc }} ...)
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[[Image:4wbc.png|left|200px|thumb|Crystal Structure of Chymotrypsin Inhibitor [[4wbc]]]]
[[Image:4wbc.png|left|200px|thumb|Crystal Structure of Chymotrypsin Inhibitor [[4wbc]]]]
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{{STRUCTURE_4wbc| PDB=4wbc | SIZE=300| SCENE= |right|CAPTION=Chymotrypsin Inhibitor [[4wbc]] }}
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{{STRUCTURE_4wbc| PDB=4wbc | SIZE=300| SCENE=Chymotrypsin_Inhibitor/Cv/1 |right|CAPTION=Chymotrypsin Inhibitor [[4wbc]] }}
[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitors]] are serine proteinase inhibitors of chymotrypsin. They are classified by numbers: CI-1, CI-2, CI-3. The images at the left and at the right correspond to one representative Chymotrypsin Inhibitor, ''i.e.'' the crystal structure of Chymotrypsin Inhibitor from ''Phosphocarpus tetragonolobus'' ([[4wbc]]).
[[Chymotrypsin Inhibitor|Chymotrypsin Inhibitors]] are serine proteinase inhibitors of chymotrypsin. They are classified by numbers: CI-1, CI-2, CI-3. The images at the left and at the right correspond to one representative Chymotrypsin Inhibitor, ''i.e.'' the crystal structure of Chymotrypsin Inhibitor from ''Phosphocarpus tetragonolobus'' ([[4wbc]]).
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=== CI-1 ===
=== CI-1 ===
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2jzm – CI-1 fragment – Nicotiana alata – NMR
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[[2jzm]] – CI-1 fragment – ''Nicotiana alata'' – NMR<br />
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1eai – CI-1+elastase - pig
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[[1eai]] – CI-1+elastase - pig
=== CI-2 ===
=== CI-2 ===
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1y1k, 1y33, 1y34, 1y3b, 1y3c, 1y3d, 1y3f, 1y48, 1y4a, 1y4d, 1tm1, 1tm3, 1tm4, 1tm5, 1tm7, 1tmg, 1to1, 1to2, 1lw6 – BaCI-2 (mutant)+subtilisin – Bacillus amyloliquefaciens
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[[1y1k]], [[1y33]], [[1y34]], [[1y3b]], [[1y3c]], [[1y3d]], [[1y3f]], [[1y48]], [[1y4a]], [[1y4d]], [[1tm1]], [[1tm3]], [[1tm4]], [[1tm5]], [[1tm7]], [[1tmg]], [[1to1]], [[1to2]], [[1lw6]] – BaCI-2 (mutant)+subtilisin – [[Bacillus amyloliquefaciens]]<br />
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2sni - BaCI-2+subtilisin
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[[2sni]] - BaCI-2+subtilisin<br />
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1ciq, 1cir– HvCI-2 fragments – Hordeum vulgare
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[[1ciq]], [[1cir]] – HvCI-2 fragments – ''Hordeum vulgare''<br />
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1coa, 1ypa, 1ypb, 1ypc – HvCI-2 (mutant)
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[[1coa]], [[1ypa]], [[1ypb]], [[1ypc]] – HvCI-2 (mutant)<br />
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1cis - HvCI-2+subtilisin helix – NMR
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[[1cis]] - HvCI-2+subtilisin helix – NMR<br />
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3ci2 - HvCI-2 – NMR
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[[3ci2]] - HvCI-2 – NMR<br />
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2ci2 - HvCI-2
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[[2ci2]] - HvCI-2
=== CI-3 ===
=== CI-3 ===
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3i2a, 3i2x, 2bea, 2beb, 2esu, 2et2, 1xg6, 1fmz, 1fn0, 1eyl – PtCI-3 (mutant) – Phosphocarpus tetragonolobus
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[[3i2a]], [[3i2x]], [[2bea]], [[2beb]], [[2esu]], [[2et2]], [[1xg6]], [[1fmz]], [[1fn0]], [[1eyl]] – PtCI-3 (mutant) – ''Phosphocarpus tetragonolobus''<br />
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4wbc, 2wbc, 1wbc - PtCI-3
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[[4wbc]], [[2wbc]], [[1wbc]] - PtCI-3<br />
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2qyi – CI-3 (mutant)+cationic trypsin – cow
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[[2qyi]] – CI-3 (mutant)+cationic trypsin – cow<br />
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[[1ccv]] – CI –''Apis mellifera'' - NMR
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1ccv – CI –Apis mellifera - NMR
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Revision as of 08:58, 13 December 2010

Image:4wbc.png
Crystal Structure of Chymotrypsin Inhibitor 4wbc

Template:STRUCTURE 4wbc

Chymotrypsin Inhibitors are serine proteinase inhibitors of chymotrypsin. They are classified by numbers: CI-1, CI-2, CI-3. The images at the left and at the right correspond to one representative Chymotrypsin Inhibitor, i.e. the crystal structure of Chymotrypsin Inhibitor from Phosphocarpus tetragonolobus (4wbc).

Contents

3D Structures of Chymotrypsin Inhibitor

CI-1

2jzm – CI-1 fragment – Nicotiana alata – NMR
1eai – CI-1+elastase - pig


CI-2

1y1k, 1y33, 1y34, 1y3b, 1y3c, 1y3d, 1y3f, 1y48, 1y4a, 1y4d, 1tm1, 1tm3, 1tm4, 1tm5, 1tm7, 1tmg, 1to1, 1to2, 1lw6 – BaCI-2 (mutant)+subtilisin – Bacillus amyloliquefaciens
2sni - BaCI-2+subtilisin
1ciq, 1cir – HvCI-2 fragments – Hordeum vulgare
1coa, 1ypa, 1ypb, 1ypc – HvCI-2 (mutant)
1cis - HvCI-2+subtilisin helix – NMR
3ci2 - HvCI-2 – NMR
2ci2 - HvCI-2


CI-3

3i2a, 3i2x, 2bea, 2beb, 2esu, 2et2, 1xg6, 1fmz, 1fn0, 1eyl – PtCI-3 (mutant) – Phosphocarpus tetragonolobus
4wbc, 2wbc, 1wbc - PtCI-3
2qyi – CI-3 (mutant)+cationic trypsin – cow
1ccv – CI –Apis mellifera - NMR

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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