1wo9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1wo9.jpg|left|200px]]
{{Seed}}
[[Image:1wo9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wo9|  PDB=1wo9  |  SCENE=  }}  
{{STRUCTURE_1wo9|  PDB=1wo9  |  SCENE=  }}  


'''Selective inhibition of trypsins by insect peptides: role of P6-P10 loop'''
===Selective inhibition of trypsins by insect peptides: role of P6-P10 loop===




==Overview==
<!--
PMP-D2 and HI, two peptides from Locusta migratoria, were shown to belong to the family of tight-binding protease inhibitors. However, they interact weakly with bovine trypsin (K(i) around 100 nM) despite a trypsin-specific Arg at the primary specificity site P1. Here we demonstrate that they are potent inhibitors of midgut trypsins isolated from the same insect and of a fungal trypsin from Fusarium oxysporum (K(i) &lt;or= 0.02 nM). Therefore, they display a selectivity not existing for the parent chymotrypsin inhibitor PMP-C. By NMR, we demonstrate that HI possesses a highly rigid structure similar to the crystal structure of a variant of PMP-D2 in complex with bovine alpha-chymotrypsin. The main difference with PMP-C is located in the region from residues 20 to 24 (positions P6-P10) that interacts with the loop containing Gly173 in chymotrypsin. The corresponding residue in mammalian trypsins is always a proline that may generate a steric clash with the inhibitor. The residues thought to confer selectivity were mutated with PMP-C as a model. The resulting analogue PMP-D2(K10W,P21A,W25A) loses some activity toward insect and fungal trypsins but is a more potent inhibitor of mammalian trypsins, corresponding to a decrease of selectivity. This work represents a first attempt in tuning the selectivity of natural peptidic serine protease inhibitors by mutating residues out of the reactive loop (P3-P'3).
The line below this paragraph, {{ABSTRACT_PUBMED_14622007}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14622007 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14622007}}


==About this Structure==
==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WO9 OCA].  
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WO9 OCA].  


==Reference==
==Reference==
Line 26: Line 30:
[[Category: Roussel, A.]]
[[Category: Roussel, A.]]
[[Category: Hydrolase inhibitor]]
[[Category: Hydrolase inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:56:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:19:32 2008''

Revision as of 13:19, 28 July 2008

File:1wo9.png

Template:STRUCTURE 1wo9

Selective inhibition of trypsins by insect peptides: role of P6-P10 loop

Template:ABSTRACT PUBMED 14622007

About this Structure

Full experimental information is available from OCA.

Reference

Selective inhibition of trypsins by insect peptides: role of P6-P10 loop., Kellenberger C, Ferrat G, Leone P, Darbon H, Roussel A, Biochemistry. 2003 Nov 25;42(46):13605-12. PMID:14622007

Page seeded by OCA on Mon Jul 28 16:19:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1wo9&oldid=706698"