1mct
From Proteopedia
(New page: 200px<br /><applet load="1mct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mct, resolution 1.6Å" /> '''THE REFINED 1.6 ANGST...) |
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| - | [[Image:1mct.jpg|left|200px]]<br /><applet load="1mct" size=" | + | [[Image:1mct.jpg|left|200px]]<br /><applet load="1mct" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mct, resolution 1.6Å" /> | caption="1mct, resolution 1.6Å" /> | ||
'''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'''<br /> | '''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'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the complex formed by porcine beta-trypsin with | + | 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 Structure== | ==About this Structure== | ||
| - | 1MCT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1MCT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MCT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: complex(proteinase/inhibitor)]] | [[Category: complex(proteinase/inhibitor)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:57 2008'' |
Revision as of 11:53, 21 February 2008
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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
Overview
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 Structure
1MCT is a Protein complex structure of sequences from Momordica charantia and Sus scrofa with as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
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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