1dg2

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(New page: 200px<br /><applet load="1dg2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg2" /> '''SOLUTION CONFORMATION OF A-CONOTOXIN AUIB'''...)
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[[Image:1dg2.gif|left|200px]]<br /><applet load="1dg2" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION CONFORMATION OF A-CONOTOXIN AUIB'''<br />
'''SOLUTION CONFORMATION OF A-CONOTOXIN AUIB'''<br />
==Overview==
==Overview==
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The neuronal nicotinic acetylcholine receptors constitute a highly diverse, group, with subtypes consisting of pentameric combinations of alpha and, beta subunits. alpha-Conotoxins are a homologous series of small peptides, that antagonize these receptors. We present the three-dimensional solution, structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin, known to selectively block the alpha(3)beta(4) nicotinic acetylcholine, receptor subtype. The pairwise backbone and heavy-atom root mean square, deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles, that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of, Tyr(15), normally present in other alpha4/7 members, results in tight, bending of the backbone at the C terminus and effectively renders Asp(14), to assume the spatial location of Tyr(15) present in other neuronal, alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB, with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows, different electrostatic surface charge distributions, which may be, important in differential receptor subtype recognition.
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The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of alpha and beta subunits. alpha-Conotoxins are a homologous series of small peptides that antagonize these receptors. We present the three-dimensional solution structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin known to selectively block the alpha(3)beta(4) nicotinic acetylcholine receptor subtype. The pairwise backbone and heavy-atom root mean square deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of Tyr(15), normally present in other alpha4/7 members, results in tight bending of the backbone at the C terminus and effectively renders Asp(14) to assume the spatial location of Tyr(15) present in other neuronal alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows different electrostatic surface charge distributions, which may be important in differential receptor subtype recognition.
==About this Structure==
==About this Structure==
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1DG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_aulicus Conus aulicus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DG2 OCA].
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1DG2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_aulicus Conus aulicus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DG2 OCA].
==Reference==
==Reference==
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[[Category: Conus aulicus]]
[[Category: Conus aulicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cho, J.H.]]
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[[Category: Cho, J H.]]
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[[Category: Han, K.H.]]
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[[Category: Han, K H.]]
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[[Category: McIntosh, J.M.]]
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[[Category: McIntosh, J M.]]
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[[Category: Mok, K.H.]]
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[[Category: Mok, K H.]]
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[[Category: Olivera, B.M.]]
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[[Category: Olivera, B M.]]
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[[Category: Park, K.H.]]
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[[Category: Park, K H.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: a-helix]]
[[Category: a-helix]]
[[Category: two disulfide bonds and c-term amidation]]
[[Category: two disulfide bonds and c-term amidation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:15:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:18 2008''

Revision as of 10:16, 21 February 2008


1dg2

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SOLUTION CONFORMATION OF A-CONOTOXIN AUIB

Overview

The neuronal nicotinic acetylcholine receptors constitute a highly diverse group, with subtypes consisting of pentameric combinations of alpha and beta subunits. alpha-Conotoxins are a homologous series of small peptides that antagonize these receptors. We present the three-dimensional solution structure of alpha-conotoxin AuIB, the first 15-residue alpha-conotoxin known to selectively block the alpha(3)beta(4) nicotinic acetylcholine receptor subtype. The pairwise backbone and heavy-atom root mean square deviation for an ensemble of 20 structures are 0.269 and 0.720 A, respectively. The overall fold of alpha-conotoxin AuIB closely resembles that of the alpha4/7 subfamily alpha-conotoxins. However, the absence of Tyr(15), normally present in other alpha4/7 members, results in tight bending of the backbone at the C terminus and effectively renders Asp(14) to assume the spatial location of Tyr(15) present in other neuronal alpha4/7 alpha-conotoxins. Structural comparison of alpha-conotoxin AuIB with the alpha(3)beta(2) subtype-specific alpha-conotoxin MII shows different electrostatic surface charge distributions, which may be important in differential receptor subtype recognition.

About this Structure

1DG2 is a Single protein structure of sequence from Conus aulicus with as ligand. Full crystallographic information is available from OCA.

Reference

Nuclear magnetic resonance solution conformation of alpha-conotoxin AuIB, an alpha(3)beta(4) subtype-selective neuronal nicotinic acetylcholine receptor antagonist., Cho JH, Mok KH, Olivera BM, McIntosh JM, Park KH, Han KH, J Biol Chem. 2000 Mar 24;275(12):8680-5. PMID:10722709

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