1ls8

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(New page: 200px<br /><applet load="1ls8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ls8" /> '''NMR structure of the unliganded Bombyx mori ...)
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[[Image:1ls8.gif|left|200px]]<br /><applet load="1ls8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ls8.gif|left|200px]]<br /><applet load="1ls8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ls8" />
caption="1ls8" />
'''NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH'''<br />
'''NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH'''<br />
==Overview==
==Overview==
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The nuclear magnetic resonance structure of the unliganded, pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide, bridges 19-54, 50-108, and 97-117. This polypeptide fold encloses a large, hydrophobic cavity, with a sufficient volume to accommodate the natural, ligand bombykol. The polypeptide folds in free BmPBP(B) and in crystals of, a BmPBP-bombykol complex are nearly identical, indicating that the B-form, of BmPBP in solution represents the active conformation for ligand, binding.
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The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide bridges 19-54, 50-108, and 97-117. This polypeptide fold encloses a large hydrophobic cavity, with a sufficient volume to accommodate the natural ligand bombykol. The polypeptide folds in free BmPBP(B) and in crystals of a BmPBP-bombykol complex are nearly identical, indicating that the B-form of BmPBP in solution represents the active conformation for ligand binding.
==About this Structure==
==About this Structure==
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1LS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LS8 OCA].
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1LS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LS8 OCA].
==Reference==
==Reference==
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[[Category: Guntert, P.]]
[[Category: Guntert, P.]]
[[Category: Horst, R.]]
[[Category: Horst, R.]]
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[[Category: Leal, W.S.]]
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[[Category: Leal, W S.]]
[[Category: Lee, D.]]
[[Category: Lee, D.]]
[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
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[[Category: solution structure]]
[[Category: solution structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:49:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:56 2008''

Revision as of 11:47, 21 February 2008


1ls8

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NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH

Overview

The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide bridges 19-54, 50-108, and 97-117. This polypeptide fold encloses a large hydrophobic cavity, with a sufficient volume to accommodate the natural ligand bombykol. The polypeptide folds in free BmPBP(B) and in crystals of a BmPBP-bombykol complex are nearly identical, indicating that the B-form of BmPBP in solution represents the active conformation for ligand binding.

About this Structure

1LS8 is a Single protein structure of sequence from Bombyx mori. Full crystallographic information is available from OCA.

Reference

NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH., Lee D, Damberger FF, Peng G, Horst R, Guntert P, Nikonova L, Leal WS, Wuthrich K, FEBS Lett. 2002 Nov 6;531(2):314-8. PMID:12417333

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