1mct: Difference between revisions

Revision as of 14:53, 21 February 2008

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 with as ligand. Active as Trypsin, with EC number 3.4.21.4 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

Page seeded by OCA on Thu Feb 21 13:53:57 2008

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-[[Image:1mct.jpg|left|200px]]<br /><applet load="1mct" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1mct.jpg|left|200px]]<br /><applet load="1mct" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1mct, resolution 1.6&Aring;" />
 '''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==
-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.
+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==
-MCT 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MCT OCA].
+MCT 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==
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 [[Category: complex(proteinase/inhibitor)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:19:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:57 2008''