1qwv: Difference between revisions

Revision as of 14:49, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qwv.png

Template:STRUCTURE 1qwv

Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)

Template:ABSTRACT PUBMED 15003458

About this StructureAbout this Structure

1QWV is a Single protein structure of sequence from Antheraea polyphemus. Full experimental information is available from OCA.

ReferenceReference

The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins., Mohanty S, Zubkov S, Gronenborn AM, J Mol Biol. 2004 Mar 19;337(2):443-51. PMID:15003458

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)'''
+===Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)===
-==Overview==
+<!--
-Pheromone-binding proteins (PBPs) located in the antennae of male moth species play an important role in olfaction. They are carrier proteins, believed to transport volatile hydrophobic pheromone molecules across the aqueous sensillar lymph to the membrane-bound G protein-coupled olfactory receptor proteins. The roles of PBPs in molecular recognition and the mechanisms of pheromone binding and release are poorly understood. Here, we report the NMR structure of a PBP from the giant silk moth Antheraea polyphemus. This is the first structure of a PBP with specific acetate-binding function in vivo. The protein consists of nine alpha-helices: alpha1a (residues 2-5), alpha1b (8-12), alpha1c (16-23), alpha2 (27-34), alpha3a (46-52), alpha3b (54-59), alpha4 (70-79), alpha5 (84-100) and alpha6 (107-125), held together by three disulfide bridges: 19-54, 50-108 and 97-117. A large hydrophobic cavity is located inside the protein, lined with side-chains from all nine helices. The acetate-binding site is located at the narrow end of the cavity formed by the helices alpha3b and alpha4. The pheromone can enter this cavity through an opening between the helix alpha1a, the C-terminal end of the helix alpha6, and the loop between alpha2 and alpha3a. We suggest that Trp37 may play an important role in the initial interaction with the ligand. Our analysis also shows that Asn53 plays the key role in recognition of acetate pheromones specifically, while Phe12, Phe36, Trp37, Phe76, and Phe118 are responsible for non-specific binding, and Leu8 and Ser9 may play a role in ligand chain length recognition.
+The line below this paragraph, {{ABSTRACT_PUBMED_15003458}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15003458}}
 ==About this Structure==
-QWV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Antheraea_polyphemus Antheraea polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWV OCA].
+QWV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Antheraea_polyphemus Antheraea polyphemus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWV OCA].
 ==Reference==
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 [[Category: Pbp fold]]
 [[Category: Pheromone binding protein]]
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