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.


1c3y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1c3y.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1c3y.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1c3y| PDB=1c3y | SCENE= }}
{{STRUCTURE_1c3y| PDB=1c3y | SCENE= }}
-
'''THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM'''
+
===THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM===
-
==Overview==
+
<!--
-
BACKGROUND: THP12 is an abundant and extraordinarily hydrophilic hemolymph protein from the mealworm Tenebrio molitor and belongs to a group of small insect proteins with four highly conserved cysteine residues. Despite their sequence homology to odorant-binding proteins and pheromone-binding proteins, the function of these proteins is unclear. RESULTS: The first three-dimensional structure of THP12 has been determined by multidimensional NMR spectroscopy. The protein has a nonbundle helical structure consisting of six alpha helices. The arrangement of the alpha helices has a 'baseball glove' shape. In addition to the hydrophobic core, electrostatic interactions make contributions to the overall stability of the protein. NMR binding studies demonstrated the binding of small hydrophobic ligands to the single hydrophobic groove in THP12. Comparing the structure of THP12 with the predicted secondary structure of homologs reveals a common fold for this new class of insect proteins. A search with the program DALI revealed extensive similarity between the three-dimensional structure of THP12 and the N-terminal domain (residues 1-95) of recoverin, a member of the family of calcium-binding EF-hand proteins. CONCLUSIONS: Although the biological function of this new class of proteins is as yet undetermined, a general role as alpha-helical carrier proteins for small hydrophobic ligands, such as fatty acids or pheromones, is proposed on the basis of NMR-shift perturbation spectroscopy.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10574794}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10574794 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10574794}}
==About this Structure==
==About this Structure==
-
1C3Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3Y OCA].
+
1C3Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tenebrio_molitor Tenebrio molitor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3Y OCA].
==Reference==
==Reference==
Line 25: Line 29:
[[Category: All-alpha]]
[[Category: All-alpha]]
[[Category: Ef-hand]]
[[Category: Ef-hand]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:18:10 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:10:45 2008''

Revision as of 17:10, 30 June 2008

Image:1c3y.png

Template:STRUCTURE 1c3y

THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM

Template:ABSTRACT PUBMED 10574794

About this Structure

1C3Y is a Single protein structure of sequence from Tenebrio molitor. Full experimental information is available from OCA.

Reference

A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands., Rothemund S, Liou YC, Davies PL, Krause E, Sonnichsen FD, Structure. 1999 Nov 15;7(11):1325-32. PMID:10574794

Page seeded by OCA on Mon Jun 30 20:10:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1c3y"
Personal tools