1f2s

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(New page: 200px<br /><applet load="1f2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2s, resolution 1.79&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1f2s.jpg|left|200px]]<br /><applet load="1f2s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f2s, resolution 1.79&Aring;" />
caption="1f2s, resolution 1.79&Aring;" />
'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION'''<br />
==Overview==
==Overview==
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The stoichiometric complex formed between bovine beta-trypsin and, Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was, crystallized and its X-ray crystal structure was refined to a final R, value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with, results on the complex of MCTI-A with porcine trypsin gives the sequence, of MCTI-A definitely, of which 13 residues are conserved compared with, other squash family trypsin inhibitors. Its spatial structure and the, conformation of its primary binding segment from Cys3I (P3) to Glu7I, (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found, to be very similar to the other squash family proteinase inhibitors.
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The stoichiometric complex formed between bovine beta-trypsin and Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was crystallized and its X-ray crystal structure was refined to a final R value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with results on the complex of MCTI-A with porcine trypsin gives the sequence of MCTI-A definitely, of which 13 residues are conserved compared with other squash family trypsin inhibitors. Its spatial structure and the conformation of its primary binding segment from Cys3I (P3) to Glu7I (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found to be very similar to the other squash family proteinase inhibitors.
==About this Structure==
==About this Structure==
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1F2S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1MCU. 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=1F2S OCA].
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1F2S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1MCU. 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=1F2S OCA].
==Reference==
==Reference==
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[[Category: trypsin]]
[[Category: trypsin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:33:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:24 2008''

Revision as of 10:34, 21 February 2008


1f2s, resolution 1.79Å

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CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN BOVINE BETA-TRYPSIN AND MCTI-A, A TRYPSIN INHIBITOR OF SQUASH FAMILY AT 1.8 A RESOLUTION

Overview

The stoichiometric complex formed between bovine beta-trypsin and Momordica charantia, Linn. Cucurbitaceae trypsin inhibitor A (MCTI-A) was crystallized and its X-ray crystal structure was refined to a final R value of 0.179 using data of 7.0- to 1.8-A resolution. Combination with results on the complex of MCTI-A with porcine trypsin gives the sequence of MCTI-A definitely, of which 13 residues are conserved compared with other squash family trypsin inhibitors. Its spatial structure and the conformation of its primary binding segment from Cys3I (P3) to Glu7I (P3'), which contains a reactive scissile bond Arg5I C-Ile6I N, were found to be very similar to the other squash family proteinase inhibitors.

About this Structure

1F2S is a Protein complex structure of sequences from Bos taurus and Momordica charantia with as ligand. This structure supersedes the now removed PDB entry 1MCU. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution., Zhu Y, Huang Q, Qian M, Jia Y, Tang Y, J Protein Chem. 1999 Jul;18(5):505-9. PMID:10524768

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