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1fny

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(New page: 200px<br /><applet load="1fny" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fny, resolution 1.81&Aring;" /> '''LEGUME LECTIN OF THE...)
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[[Image:1fny.gif|left|200px]]<br /><applet load="1fny" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fny.gif|left|200px]]<br /><applet load="1fny" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fny, resolution 1.81&Aring;" />
caption="1fny, resolution 1.81&Aring;" />
'''LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.'''<br />
'''LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.'''<br />
==Overview==
==Overview==
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The structure of the bark lectin RPbAI (isoform A4) from Robinia, pseudoacacia has been determined by protein crystallography both in the, free form and complexed with N-acetylgalactosamine. The free form is, refined at 1.80 A resolution to an R-factor of 18.9% whereas the complexed, structure has an R-factor of 19.7% at 2.05 A resolution. Both structures, are compared to each other and to other available legume lectin, structures. The polypeptide chains of the two structures exhibit the, characteristic legume lectin tertiary fold. The quaternary structure, resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features, leading to the extreme stability of this lectin.
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The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N-acetylgalactosamine. The free form is refined at 1.80 A resolution to an R-factor of 18.9% whereas the complexed structure has an R-factor of 19.7% at 2.05 A resolution. Both structures are compared to each other and to other available legume lectin structures. The polypeptide chains of the two structures exhibit the characteristic legume lectin tertiary fold. The quaternary structure resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features leading to the extreme stability of this lectin.
==About this Structure==
==About this Structure==
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1FNY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Robinia_pseudoacacia Robinia pseudoacacia] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNY OCA].
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1FNY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Robinia_pseudoacacia Robinia pseudoacacia] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barre, A.]]
[[Category: Barre, A.]]
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[[Category: Damme, E.J.Van.]]
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[[Category: Damme, E J.Van.]]
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[[Category: Peumans, W.J.]]
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[[Category: Peumans, W J.]]
[[Category: Rabijns, A.]]
[[Category: Rabijns, A.]]
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[[Category: Ranter, C.J.De.]]
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[[Category: Ranter, C J.De.]]
[[Category: Rouge, P.]]
[[Category: Rouge, P.]]
[[Category: Verboven, C.]]
[[Category: Verboven, C.]]
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[[Category: legume lectin]]
[[Category: legume lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:04:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:41 2008''

Revision as of 10:40, 21 February 2008


1fny, resolution 1.81Å

Drag the structure with the mouse to rotate

LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.

Overview

The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N-acetylgalactosamine. The free form is refined at 1.80 A resolution to an R-factor of 18.9% whereas the complexed structure has an R-factor of 19.7% at 2.05 A resolution. Both structures are compared to each other and to other available legume lectin structures. The polypeptide chains of the two structures exhibit the characteristic legume lectin tertiary fold. The quaternary structure resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features leading to the extreme stability of this lectin.

About this Structure

1FNY is a Single protein structure of sequence from Robinia pseudoacacia with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine., Rabijns A, Verboven C, Rouge P, Barre A, Van Damme EJ, Peumans WJ, De Ranter CJ, Proteins. 2001 Sep 1;44(4):470-8. PMID:11484224

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