2cna

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(New page: 200px<br /><applet load="2cna" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cna, resolution 2.0&Aring;" /> '''THE COVALENT AND THRE...)
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[[Image:2cna.gif|left|200px]]<br /><applet load="2cna" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2cna, resolution 2.0&Aring;" />
caption="2cna, resolution 2.0&Aring;" />
'''THE COVALENT AND THREE-DIMENSIONAL STRUCTURE OF CONCANAVALIN A, IV.ATOMIC COORDINATES,HYDROGEN BONDING,AND QUATERNARY STRUCTURE'''<br />
'''THE COVALENT AND THREE-DIMENSIONAL STRUCTURE OF CONCANAVALIN A, IV.ATOMIC COORDINATES,HYDROGEN BONDING,AND QUATERNARY STRUCTURE'''<br />
==Overview==
==Overview==
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The coordinates of the individual non-hydrogen atoms of the lectin, concanavalin A have been determined from the molecular model at 2.0-A, resolution and have been adjusted to make them consistent with the known, stereochemistry of the constituent amino acid residues. From the, coordinates, an analysis has been made of all intra- and intersubunit, interactions in the molecule, yielding a description of the, hydrogen-bonded structure of the monomer, including two extensive pleated, sheet structures and other features of the folding of the polypeptide, chain. The description of the noncovalent bonding is extended to include, the interactions involved in stabilization of the dimeric and tetrameric, structures of the molecule. The complete description of the molecular, structure provides a basis for analysis of the biological activities of, concanavalin A.
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The coordinates of the individual non-hydrogen atoms of the lectin concanavalin A have been determined from the molecular model at 2.0-A resolution and have been adjusted to make them consistent with the known stereochemistry of the constituent amino acid residues. From the coordinates, an analysis has been made of all intra- and intersubunit interactions in the molecule, yielding a description of the hydrogen-bonded structure of the monomer, including two extensive pleated sheet structures and other features of the folding of the polypeptide chain. The description of the noncovalent bonding is extended to include the interactions involved in stabilization of the dimeric and tetrameric structures of the molecule. The complete description of the molecular structure provides a basis for analysis of the biological activities of concanavalin A.
==About this Structure==
==About this Structure==
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2CNA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CNA OCA].
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2CNA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canavalia_ensiformis Canavalia ensiformis] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNA OCA].
==Reference==
==Reference==
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[[Category: Canavalia ensiformis]]
[[Category: Canavalia ensiformis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Becker, J.W.]]
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[[Category: Becker, J W.]]
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[[Category: Edelman, G.M.]]
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[[Category: Edelman, G M.]]
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[[Category: Reekejunior, G.N.]]
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[[Category: Reekejunior, G N.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MN]]
[[Category: MN]]
[[Category: lectin (agglutinin)]]
[[Category: lectin (agglutinin)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:10:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:50:39 2008''

Revision as of 14:50, 21 February 2008


2cna, resolution 2.0Å

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THE COVALENT AND THREE-DIMENSIONAL STRUCTURE OF CONCANAVALIN A, IV.ATOMIC COORDINATES,HYDROGEN BONDING,AND QUATERNARY STRUCTURE

Overview

The coordinates of the individual non-hydrogen atoms of the lectin concanavalin A have been determined from the molecular model at 2.0-A resolution and have been adjusted to make them consistent with the known stereochemistry of the constituent amino acid residues. From the coordinates, an analysis has been made of all intra- and intersubunit interactions in the molecule, yielding a description of the hydrogen-bonded structure of the monomer, including two extensive pleated sheet structures and other features of the folding of the polypeptide chain. The description of the noncovalent bonding is extended to include the interactions involved in stabilization of the dimeric and tetrameric structures of the molecule. The complete description of the molecular structure provides a basis for analysis of the biological activities of concanavalin A.

About this Structure

2CNA is a Single protein structure of sequence from Canavalia ensiformis with and as ligands. Full crystallographic information is available from OCA.

Reference

The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure., Reeke GN Jr, Becker JW, Edelman GM, J Biol Chem. 1975 Feb 25;250(4):1525-47. PMID:1112816

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