This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ynl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ynl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ynl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ynl| PDB=1ynl | SCENE= }}
{{STRUCTURE_1ynl| PDB=1ynl | SCENE= }}
-
'''Identification of Key residues of the NC6.8 Fab antibody fragment binding to synthetic sweeterners: Crystal structure of NC6.8 co-crystalized with high potency sweetener compound SC45647'''
+
===Identification of Key residues of the NC6.8 Fab antibody fragment binding to synthetic sweeterners: Crystal structure of NC6.8 co-crystalized with high potency sweetener compound SC45647===
-
==Overview==
+
<!--
-
The crystal structures of the murine monoclonal IgG2b(kappa) antibody NC6.8 Fab fragment complexed with high-potency sweetener compound SC45647 and nontasting high-affinity antagonist TES have been determined. The crystal structures show how sweetener potency is fine-tuned by multiple interactions between specific receptor residues and the functionally different groups of the sweeteners. Comparative analysis with the structure of NC6.8 complexed with the super-potency sweetener NC174 reveals that although the same residues in the antigen binding pocket of NC6.8 interact with the zwitterionic, trisubstituted guanidinium sweeteners as well as TES, specific differences exist and provide guidance for the design of new artificial sweeteners. In case of the nonsweetener TES, the interactions with the receptor are indirectly mediated through a hydrogen bonded water network, while the sweeteners bind with high affinity directly to the receptor. The presence of a hydrophobic group interacting with multiple receptor residues as a major determinant for sweet taste has been confirmed. The nature of the hydrophobic group is likely a discriminator for super- versus high-potency sweeteners, which can be exploited in the design of new, highly potent sweetener compounds. Overall similarities and partial conservation of interactions indicate that the NC6.8 Fab surrogate is representing crucial features of the T1R2 taste receptor VFTM binding site.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16026161}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16026161 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16026161}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Sweetener compound]]
[[Category: Sweetener compound]]
[[Category: Triethyl aminomethane sulfonyl acid]]
[[Category: Triethyl aminomethane sulfonyl acid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:33:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:25:56 2008''

Revision as of 18:26, 28 July 2008

Image:1ynl.png

Template:STRUCTURE 1ynl

Identification of Key residues of the NC6.8 Fab antibody fragment binding to synthetic sweeterners: Crystal structure of NC6.8 co-crystalized with high potency sweetener compound SC45647

Template:ABSTRACT PUBMED 16026161

About this Structure

Full crystallographic information is available from OCA.

Reference

Cocrystal structures of NC6.8 Fab identify key interactions for high potency sweetener recognition: implications for the design of synthetic sweeteners., Gokulan K, Khare S, Ronning DR, Linthicum SD, Sacchettini JC, Rupp B, Biochemistry. 2005 Jul 26;44(29):9889-98. PMID:16026161

Page seeded by OCA on Mon Jul 28 21:25:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ynl"
Personal tools