1gm2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1gm2.jpg|left|200px]]
{{Seed}}
[[Image:1gm2.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gm2|  PDB=1gm2  |  SCENE=  }}  
{{STRUCTURE_1gm2|  PDB=1gm2  |  SCENE=  }}  


'''THE INDEPENDENT STRUCTURE OF THE ANTITRYPTIC REACTIVE SITE LOOP OF BOWMAN-BIRK INHIBITOR AND SUNFLOWER TRYPSIN INHIBITOR-1'''
===THE INDEPENDENT STRUCTURE OF THE ANTITRYPTIC REACTIVE SITE LOOP OF BOWMAN-BIRK INHIBITOR AND SUNFLOWER TRYPSIN INHIBITOR-1===




==Overview==
<!--  
Bowman-Birk inhibitor (BBI) proteins contain an inhibitory motif comprising a disulfide-bonded sequence that interacts with serine proteinases. Recently, a small 14-residue peptide from sunflowers (SFTI-1), which has potent anti-trypsin activity, has been found to have the same motif. However, this peptide also has an unusual head-to-tail cyclisation. To address the role of the core inhibitory sequence itself, we have solved the (1)H-NMR solution structure of an antitryptic 11-residue cyclic peptide that corresponds to the core reactive site loops of both SFTI-1 and Bowman-Birk inhibitor proteins. A comparison is made between the secondary chemical shifts found in this family and the canonical regions of several other inhibitors, giving some insight into relative flexibility and hydrogen bonding patterns in these inhibitors. The solution structure of the core peptide in isolation is found to retain essentially the same three-dimensional arrangement of both backbone and side chains as observed in larger antitryptic BBI and SFTI-1 fragments as well as in the complete proteins. The retention of the canonical conformation in the core peptide explains the peptids inhibitory potency. It therefore represents a minimization of both the BBI and SFTI-1 sequences. We conclude that the core peptide is a conformationally defined, canonical scaffold, which can serve as a minimal platform for the engineering of biological activity.
The line below this paragraph, {{ABSTRACT_PUBMED_12144352}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12144352 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12144352}}


==About this Structure==
==About this Structure==
1GM2 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM2 OCA].  
1GM2 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM2 OCA].  


==Reference==
==Reference==
Line 28: Line 32:
[[Category: Trypsin inhibitor]]
[[Category: Trypsin inhibitor]]
[[Category: Type vib beta-turn peptide]]
[[Category: Type vib beta-turn peptide]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:44:18 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:30:05 2008''

Revision as of 02:30, 1 July 2008

File:1gm2.png

Template:STRUCTURE 1gm2

THE INDEPENDENT STRUCTURE OF THE ANTITRYPTIC REACTIVE SITE LOOP OF BOWMAN-BIRK INHIBITOR AND SUNFLOWER TRYPSIN INHIBITOR-1

Template:ABSTRACT PUBMED 12144352

About this Structure

1GM2 is a Single protein structure. Full experimental information is available from OCA.

Reference

The (1)H-NMR solution structure of the antitryptic core peptide of Bowman-Birk inhibitor proteins: a minimal canonical loop., Brauer AB, Kelly G, Matthews SJ, Leatherbarrow RJ, J Biomol Struct Dyn. 2002 Aug;20(1):59-70. PMID:12144352

Page seeded by OCA on Tue Jul 1 05:30:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gm2&oldid=602826"