Sandbox Reserved 960
From Proteopedia
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AmelASP1 presents <scene name='60/604479/Disulfide_bonds/1'> three disulfide bridges</scene> which are greatly enhancing its structure’s rigidity by linking four of the helices together. The six cysteins and their interval spacing are the most striking features shared by proteins belonging to the PBP family. | AmelASP1 presents <scene name='60/604479/Disulfide_bonds/1'> three disulfide bridges</scene> which are greatly enhancing its structure’s rigidity by linking four of the helices together. The six cysteins and their interval spacing are the most striking features shared by proteins belonging to the PBP family. | ||
- | The <scene name='60/604479/1st_disulfide_bridge/1'>first disulfide bridge</scene> is established between <scene name='60/604479/H1/2'>H1</scene> and <scene name='60/604479/H3/2'>H3</scene> through Cysteines 20 and 51. <scene name='60/604479/2nd_disulfide_bridge/2'>An other disulfide bridge</scene> links <scene name='60/604479/H3/2'>H3</scene> and <scene name='60/604479/H7/1'>H7</scene> through Cys 47 and 98, and the <scene name='60/604479/3rd_disulfide_bridge/1'>third disulfide bridge</scene> connects <scene name='60/604479/ | + | The <scene name='60/604479/1st_disulfide_bridge/1'>first disulfide bridge</scene> is established between <scene name='60/604479/H1/2'>H1</scene> and <scene name='60/604479/H3/2'>H3</scene> through Cysteines 20 and 51. <scene name='60/604479/2nd_disulfide_bridge/2'>An other disulfide bridge</scene> links <scene name='60/604479/H3/2'>H3</scene> and <scene name='60/604479/H7/1'>H7</scene> through Cys 47 and 98, and the <scene name='60/604479/3rd_disulfide_bridge/1'>third disulfide bridge</scene> connects <scene name='60/604479/H6/1'>H6</scene> and <scene name='60/604479/H7/1'>H7</scene> thanks to Cys 89 and Cys 107. |
Furthermore, non covalent bonds also play an important role. | Furthermore, non covalent bonds also play an important role. |
Revision as of 10:49, 3 January 2015
This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975. |
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Antennal Specific Protein-1 from Apis mellifera (AmelASP1) with a serendipitous ligand at pH 5.5
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Contributors
Updated on 03-January-2015
Sophie Morin & Mathias Buytaert
References for further information on the pheromone binding protein from Apis mellifera
- ↑ http://www.genome.jp/dbget-bin/www_bget?pdb:3FE6
- ↑ Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Tegoni M, Cambillau C. Structural basis of the honey bee PBP pheromone and pH-induced conformational change. J Mol Biol. 2008 Jun 27;380(1):158-69. Epub 2008 Apr 27. PMID:18508083 doi:10.1016/j.jmb.2008.04.048
- ↑ Han L, Zhang YJ, Zhang L, Cui X, Yu J, Zhang Z, Liu MS. Operating mechanism and molecular dynamics of pheromone-binding protein ASP1 as influenced by pH. PLoS One. 2014 Oct 22;9(10):e110565. doi: 10.1371/journal.pone.0110565., eCollection 2014. PMID:25337796 doi:http://dx.doi.org/10.1371/journal.pone.0110565
- ↑ Lartigue A, Gruez A, Briand L, Blon F, Bezirard V, Walsh M, Pernollet JC, Tegoni M, Cambillau C. Sulfur single-wavelength anomalous diffraction crystal structure of a pheromone-binding protein from the honeybee Apis mellifera L. J Biol Chem. 2004 Feb 6;279(6):4459-64. Epub 2003 Oct 31. PMID:14594955 doi:10.1074/jbc.M311212200
- ↑ Pesenti ME, Spinelli S, Bezirard V, Briand L, Pernollet JC, Campanacci V, Tegoni M, Cambillau C. Queen bee pheromone binding protein pH-induced domain swapping favors pheromone release. J Mol Biol. 2009 Jul 31;390(5):981-90. Epub 2009 May 28. PMID:19481550 doi:10.1016/j.jmb.2009.05.067
- ↑ Han L, Zhang YJ, Zhang L, Cui X, Yu J, Zhang Z, Liu MS. Operating mechanism and molecular dynamics of pheromone-binding protein ASP1 as influenced by pH. PLoS One. 2014 Oct 22;9(10):e110565. doi: 10.1371/journal.pone.0110565., eCollection 2014. PMID:25337796 doi:http://dx.doi.org/10.1371/journal.pone.0110565