1mct: Difference between revisions
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|PDB= 1mct |SIZE=350|CAPTION= <scene name='initialview01'>1mct</scene>, resolution 1.6Å | |PDB= 1mct |SIZE=350|CAPTION= <scene name='initialview01'>1mct</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mct OCA], [http://www.ebi.ac.uk/pdbsum/1mct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mct RCSB]</span> | |||
}} | }} | ||
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[[Category: Liu, S.]] | [[Category: Liu, S.]] | ||
[[Category: Tang, Y.]] | [[Category: Tang, Y.]] | ||
[[Category: complex(proteinase/inhibitor)]] | [[Category: complex(proteinase/inhibitor)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:29 2008'' | ||
Revision as of 22:14, 30 March 2008
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| , resolution 1.6Å | |||||||
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| Ligands: | |||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE REFINED 1.6 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY
OverviewOverview
The crystal structure of the complex formed by porcine beta-trypsin with the MCTI-A inhibitor (Momordica charantia, Linn. Cucurbitaceae) has been determined at 1.6 A resolution using the molecular replacement method. The sequence of MCTI-A was determined by recognizing the electron density, and shows that MCTI-A is a member of the squash family of trypsin inhibitors. We report the first high-resolution structure of porcine beta-trypsin. Detailed comparisons have been made on the overall structure, solvent structure and active-site geometries between this complex and bovine beta-trypsin and its complexes. On the basis of our results, we discuss the interaction patterns between inhibitor and trypsin. Unlike other complex structures formed by bovine trypsin with inhibitors, no out-of-plane distortion around the inhibitor's scissible peptide was observed. The role of the trypsin catalytic triad is also discussed on the basis of this structure.
About this StructureAbout this Structure
1MCT is a Protein complex structure of sequences from Momordica charantia and Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex., Huang Q, Liu S, Tang Y, J Mol Biol. 1993 Feb 20;229(4):1022-36. PMID:8445634
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