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Eglin

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Current revision (17:57, 19 October 2017) (edit) (undo)
 
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[[Image:1egp.png|left|200px|thumb|Crystal Structure of Leech Eglin, [[1egp]]]]
 
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{{STRUCTURE_1egp| PDB=1egp | SIZE=300| SCENE=Eglin/Cv/1 |right|CAPTION=Cleaved leech Eglin, [[1egp]] }}
 
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[[Eglin]] C is a serine proteinase inhibitor isolated from leech. The images at the left and at the right correspond to one representative Eglin structure, ''i.e.'' crystal structure of Leech Eglin ([[1egp]]) which was cleaved between residues 45 and 46.
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<StructureSection load='1egp' size='350' side='right' caption='Cleaved leech Eglin. Residues 1-45 (grey) and 46-70 (green) (PDB code [[1egp]]).' scene='Eglin/Cv/1'>
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{{TOC limit|limit=2}}
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'''Eglin C''' is a serine proteinase inhibitor isolated from leech. <ref>PMID:3064813</ref>
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== Relevance ==
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Eglin C and its mutants are tested as protease inhibitor drugs.
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</StructureSection>
== 3D Structures of Eglin ==
== 3D Structures of Eglin ==
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[[4h4f]] - lEglin-C+ hChymotrypsin – human<br />
[[4h4f]] - lEglin-C+ hChymotrypsin – human<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Cleaved leech Eglin. Residues 1-45 (grey) and 46-70 (green) (PDB code 1egp).

Drag the structure with the mouse to rotate

3D Structures of Eglin

Updated on 19-October-2017

1egp – lEglin-C – leech
1egl - lEglin-C – NMR
1sbn, 1sib, 1cse - lEglin-C+BsSubtilisin – Bacillus subtilis
2sec - lEglin-C+BlSubtilisin – Bacillus licheniformis
1acb - lEglin-C+bChymotrypsinogen – bovine
4b1t, 4b2a, 4b2b, 4b2c - lEglin-C (mutant) +bTrypsin (mutant)
1mee - lEglin-C+BpMesentericopeptidase – Bacillus pumilus
2tec, 3tec, 1tec - lEglin-C+TvThermitase – Thermoactinomyces vulgaris
4h4f - lEglin-C+ hChymotrypsin – human

References

  1. ↑ McPhalen CA, James MN. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry. 1988 Aug 23;27(17):6582-98. PMID:3064813

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Jaime Prilusky

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