1f34: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN== | ==CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN== | ||
<StructureSection load='1f34' size='340' side='right' caption='[[1f34]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='1f34' size='340' side='right'caption='[[1f34]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascsu Ascsu] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F34 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascsu Ascsu] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F34 FirstGlance]. <br> | ||
| Line 39: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ascsu]] | [[Category: Ascsu]] | ||
[[Category: Large Structures]] | |||
[[Category: Pepsin A]] | [[Category: Pepsin A]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
Revision as of 13:35, 8 January 2020
CRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSINCRYSTAL STRUCTURE OF ASCARIS PEPSIN INHIBITOR-3 BOUND TO PORCINE PEPSIN
Structural highlights
Function[PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. [API3_ASCSU] This is an inhibitor of the aspartic protease pepsin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and 2.45 A resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this unique inhibitor. PI-3 has a new fold consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the 'active site flap' (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that spans the two proteins. PI-3 has a novel mode of inhibition, using its N-terminal residues to occupy and therefore block the first three binding pockets in pepsin for substrate residues C-terminal to the scissile bond (S1'-S3'). The molecular structure of the pepsin-PI-3 complex suggests new avenues for the rational design of proteinaceous aspartic proteinase inhibitors. Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.,Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN Nat Struct Biol. 2000 Aug;7(8):653-7. PMID:10932249[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||||