1mtn

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(New page: 200px<br /><applet load="1mtn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mtn, resolution 2.8&Aring;" /> '''BOVINE ALPHA-CHYMOTRY...)
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[[Image:1mtn.gif|left|200px]]<br /><applet load="1mtn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mtn, resolution 2.8&Aring;" />
caption="1mtn, resolution 2.8&Aring;" />
'''BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION'''<br />
'''BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION'''<br />
==Overview==
==Overview==
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The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex, with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved, and refined at 2.8 A resolution (R-factor = 0.18). The, proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two, BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is, contacting both proteinase molecules in the dimer, through the reactive, site loop and through residues next to the inhibitor's C-terminal region., Specific recognition between alpha-CHT and BPTI occurs at the (re)active, site interface according to structural rules inferred from the analysis of, homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of, BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being, hydrogen bonded to backbone atoms of the enzyme surface residues Gly216, and Ser217.
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The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 A resolution (R-factor = 0.18). The proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between alpha-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217.
==About this Structure==
==About this Structure==
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1MTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MTN OCA].
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1MTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MTN 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 21:41:19 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:51 2008''

Revision as of 11:59, 21 February 2008

Image:1mtn.gif

1mtn, resolution 2.8Å

Drag the structure with the mouse to rotate

BOVINE ALPHA-CHYMOTRYPSIN:BPTI CRYSTALLIZATION

Overview

The crystal structure of bovine alpha-chymotrypsin (alpha-CHT) in complex with the bovine basic pancreatic trypsin inhibitor (BPTI) has been solved and refined at 2.8 A resolution (R-factor = 0.18). The proteinase:inhibitor complex forms a compact dimer (two alpha-CHT and two BPTI molecules), which may be stabilized by surface-bound sulphate ions, in the crystalline state. Each BPTI molecule, at opposite ends, is contacting both proteinase molecules in the dimer, through the reactive site loop and through residues next to the inhibitor's C-terminal region. Specific recognition between alpha-CHT and BPTI occurs at the (re)active site interface according to structural rules inferred from the analysis of homologous serine proteinase:inhibitor complexes. Lys15, the P1 residue of BPTI, however, does not occupy the alpha-CHT S1 specificity pocket, being hydrogen bonded to backbone atoms of the enzyme surface residues Gly216 and Ser217.

About this Structure

1MTN is a Protein complex structure of sequences from Bos taurus with as ligand. Active as Chymotrypsin, with EC number 3.4.21.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the bovine alpha-chymotrypsin:Kunitz inhibitor complex. An example of multiple protein:protein recognition sites., Capasso C, Rizzi M, Menegatti E, Ascenzi P, Bolognesi M, J Mol Recognit. 1997 Jan-Feb;10(1):26-35. PMID:9179777

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