2gnt: Difference between revisions

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[[Image:2gnt.~~gif~~|left|200px]]

[[Image:2gnt.png|left|200px]]

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~~'''~~EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)~~'''~~

===EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)===

~~==Overview==~~

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The ~~interplay between metal binding~~, ~~carbohydrate binding activity~~, ~~stability and structure of~~ the ~~lectin from Pterocarpus angolensis was investigated. Removal of the metals leads~~ to ~~a more flexible form of~~ the ~~protein with significantly less conformational stability~~. ~~Crystal structures of this metal-free form show significant structural rearrangements~~, ~~although some structural features that allow~~ the ~~binding of sugars are retained~~. ~~We propose that substitution of an asparagine residue at the start of the C~~-~~terminal beta~~-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.

The line below this paragraph, {{ABSTRACT_PUBMED_16824540}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16824540 is the PubMed ID number.

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==About this Structure==

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[[Category: Pal]]

[[Category: Remetallization]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 05~~:19:12 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:52:43 2008''

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-[[Image:2gnt.gif|left|200px]]
+{{Seed}}
+[[Image:2gnt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2gnt|  PDB=2gnt  |  SCENE=  }}
-'''EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)'''
+===EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)===
-==Overview==
+<!--
-The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.
+The line below this paragraph, {{ABSTRACT_PUBMED_16824540}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16824540 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16824540}}
 ==About this Structure==
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 [[Category: Pal]]
 [[Category: Remetallization]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:19:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:52:43 2008''