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.

1dqe

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:55, 13 December 2017

BOMBYX MORI PHEROMONE BINDING PROTEIN

Structural highlights

1dqe is a 2 chain structure with sequence from Bommo. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PBP_BOMMO] This major soluble protein in olfactory sensilla of male moths serves to solubilize the extremely hydrophobic pheromone molecules such as bombykol and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Insects use volatile organic molecules to communicate messages with remarkable sensitivity and specificity. In one of the most studied systems, female silkworm moths (Bombyx mori) attract male mates with the pheromone bombykol, a volatile 16-carbon alcohol. In the male moth's antennae, a pheromone-binding protein conveys bombykol to a membrane-bound receptor on a nerve cell. The structure of the pheromone-binding protein, its binding and recognition of bombykol, and its full role in signal transduction are not known. RESULTS: The three-dimensional structure of the B. mori pheromone-binding protein with bound bombykol has been determined by X-ray diffraction at 1.8 A resolution. CONCLUSIONS: The pheromone binding protein of B. mori has six helices, and bombykol binds in a completely enclosed hydrophobic cavity formed by four antiparallel helices. Bombykol is bound in this cavity through numerous hydrophobic interactions, and sequence alignments suggest critical residues for specific pheromone binding.

Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex.,Sandler BH, Nikonova L, Leal WS, Clardy J Chem Biol. 2000 Feb;7(2):143-51. PMID:10662696^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sandler BH, Nikonova L, Leal WS, Clardy J. Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex. Chem Biol. 2000 Feb;7(2):143-51. PMID:10662696

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dqe"

@@ Line 1: / Line 1: @@
 ==BOMBYX MORI PHEROMONE BINDING PROTEIN==
 <StructureSection load='1dqe' size='340' side='right' caption='[[1dqe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1dqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bommo Bommo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DQE FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOM:HEXADECA-10,12-DIEN-1-OL'>BOM</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqe OCA], [http://pdbe.org/1dqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dqe RCSB], [http://www.ebi.ac.uk/pdbsum/1dqe PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dqe OCA], [http://pdbe.org/1dqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dqe RCSB], [http://www.ebi.ac.uk/pdbsum/1dqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dqe ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqe_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dq/1dqe_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1dqe

From Proteopedia

Revision as of 07:55, 13 December 2017

BOMBYX MORI PHEROMONE BINDING PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox