1mcv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1mcv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mcv, resolution 1.8&Aring;" /> '''Crystal Structure Ana...)
Line 1: Line 1:
-
[[Image:1mcv.jpg|left|200px]]<br /><applet load="1mcv" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1mcv.jpg|left|200px]]<br /><applet load="1mcv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mcv, resolution 1.8&Aring;" />
caption="1mcv, resolution 1.8&Aring;" />
'''Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase'''<br />
'''Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase'''<br />
==Overview==
==Overview==
-
The crystal structure of porcine pancreatic elastase in complex with a, hybrid squash inhibitor (HEI-TOE I; 28 amino acids) has been determined to, a resolution of 1.8 A. To construct the hybrid inhibitor, the, trypsin-binding loop of the squash inhibitor from Ecballium elaterium was, substituted by the sequence of a peptide that was derived from the third, domain of the turkey ovomucoid inhibitor and was optimized to inhibit, porcine pancreatic elastase. This modification of the squash inhibitor, changed its specificity for trypsin to a specificity for porcine, pancreatic elastase. Specific interactions of this hybrid inhibitor with, porcine pancreatic elastase and the differences from the interactions of, the ovomucoid inhibitor with human leukocyte elastase are discussed. The, binding loop of the inhibitor adopts a 'canonical' conformation and the, scissile bond Leu-Glu remains intact.
+
The crystal structure of porcine pancreatic elastase in complex with a hybrid squash inhibitor (HEI-TOE I; 28 amino acids) has been determined to a resolution of 1.8 A. To construct the hybrid inhibitor, the trypsin-binding loop of the squash inhibitor from Ecballium elaterium was substituted by the sequence of a peptide that was derived from the third domain of the turkey ovomucoid inhibitor and was optimized to inhibit porcine pancreatic elastase. This modification of the squash inhibitor changed its specificity for trypsin to a specificity for porcine pancreatic elastase. Specific interactions of this hybrid inhibitor with porcine pancreatic elastase and the differences from the interactions of the ovomucoid inhibitor with human leukocyte elastase are discussed. The binding loop of the inhibitor adopts a 'canonical' conformation and the scissile bond Leu-Glu remains intact.
==About this Structure==
==About this Structure==
-
1MCV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MCV OCA].
+
1MCV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MCV OCA].
==Reference==
==Reference==
Line 24: Line 24:
[[Category: hybrid squash inhibitor]]
[[Category: hybrid squash inhibitor]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:19:59 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:58 2008''

Revision as of 11:54, 21 February 2008


1mcv, resolution 1.8Å

Drag the structure with the mouse to rotate

Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase

Overview

The crystal structure of porcine pancreatic elastase in complex with a hybrid squash inhibitor (HEI-TOE I; 28 amino acids) has been determined to a resolution of 1.8 A. To construct the hybrid inhibitor, the trypsin-binding loop of the squash inhibitor from Ecballium elaterium was substituted by the sequence of a peptide that was derived from the third domain of the turkey ovomucoid inhibitor and was optimized to inhibit porcine pancreatic elastase. This modification of the squash inhibitor changed its specificity for trypsin to a specificity for porcine pancreatic elastase. Specific interactions of this hybrid inhibitor with porcine pancreatic elastase and the differences from the interactions of the ovomucoid inhibitor with human leukocyte elastase are discussed. The binding loop of the inhibitor adopts a 'canonical' conformation and the scissile bond Leu-Glu remains intact.

About this Structure

1MCV is a Single protein structure of sequence from Sus scrofa with and as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.

Reference

Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution., Ay J, Hilpert K, Krauss N, Schneider-Mergener J, Hohne W, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):247-54. Epub 2003, Jan 23. PMID:12554935

Page seeded by OCA on Thu Feb 21 13:53:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools