1aj3: Difference between revisions

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[[Image:1aj3.gif|left|200px]]<br /><applet load="1aj3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1aj3.gif|left|200px]]<br /><applet load="1aj3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1aj3" />

'''SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES'''<br />

==Overview==

Cytoskeletal proteins belonging to the spectrin family have an elongated, structure composed of repetitive units. The three-dimensional solution, structure of the 16th repeat from chicken brain alpha-spectrin (R16) has, been determined by NMR spectroscopy and distance geometry-simulated, annealing calculations. We used a total of 1035 distance restraints, which, included 719 NOE-based values obtained by applying the ambiguous, restraints for iterative assignment (ARIA) method. In addition, we, performed a direct refinement against 1H-chemical shifts. The final, ensemble of 20 structures shows an average RMSD of 1.52 A from the mean, for the backbone atoms, excluding loops and N and C termini. R16 is made, up of three antiparallel alpha-helices separated by two loops, and folds, into a left-handed coiled-coil.The basic unit of spectrin is an, antiparallel heterodimer composed of two homologous chains, beta and, alpha. These assemble a tetramer via a mechanism that relies on the, completion of a single repeat by association of the partial repeats, located at the C terminus of the beta-chain (two helices) and at the N, terminus of the alpha-chain (one helix). This tetramer is the assemblage, able to cross-link actin filaments. Model building by homology of the, "tetramerization" repeat from human erythrocyte spectrin illuminates the, possible role of point mutations which cause hemolytic anemias.

Cytoskeletal proteins belonging to the spectrin family have an elongated structure composed of repetitive units. The three-dimensional solution structure of the 16th repeat from chicken brain alpha-spectrin (R16) has been determined by NMR spectroscopy and distance geometry-simulated annealing calculations. We used a total of 1035 distance restraints, which included 719 NOE-based values obtained by applying the ambiguous restraints for iterative assignment (ARIA) method. In addition, we performed a direct refinement against 1H-chemical shifts. The final ensemble of 20 structures shows an average RMSD of 1.52 A from the mean for the backbone atoms, excluding loops and N and C termini. R16 is made up of three antiparallel alpha-helices separated by two loops, and folds into a left-handed coiled-coil.The basic unit of spectrin is an antiparallel heterodimer composed of two homologous chains, beta and alpha. These assemble a tetramer via a mechanism that relies on the completion of a single repeat by association of the partial repeats located at the C terminus of the beta-chain (two helices) and at the N terminus of the alpha-chain (one helix). This tetramer is the assemblage able to cross-link actin filaments. Model building by homology of the "tetramerization" repeat from human erythrocyte spectrin illuminates the possible role of point mutations which cause hemolytic anemias.

==About this Structure==

1AJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1AJ3 OCA].

1AJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ3 OCA].

==Reference==

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[[Category: spectrin]]

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@@ Line 1: / Line 1: @@
-[[Image:1aj3.gif|left|200px]]<br /><applet load="1aj3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1aj3.gif|left|200px]]<br /><applet load="1aj3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1aj3" />
 '''SOLUTION STRUCTURE OF THE SPECTRIN REPEAT, NMR, 20 STRUCTURES'''<br />
 ==Overview==
-Cytoskeletal proteins belonging to the spectrin family have an elongated, structure composed of repetitive units. The three-dimensional solution, structure of the 16th repeat from chicken brain alpha-spectrin (R16) has, been determined by NMR spectroscopy and distance geometry-simulated, annealing calculations. We used a total of 1035 distance restraints, which, included 719 NOE-based values obtained by applying the ambiguous, restraints for iterative assignment (ARIA) method. In addition, we, performed a direct refinement against 1H-chemical shifts. The final, ensemble of 20 structures shows an average RMSD of 1.52 A from the mean, for the backbone atoms, excluding loops and N and C termini. R16 is made, up of three antiparallel alpha-helices separated by two loops, and folds, into a left-handed coiled-coil.The basic unit of spectrin is an, antiparallel heterodimer composed of two homologous chains, beta and, alpha. These assemble a tetramer via a mechanism that relies on the, completion of a single repeat by association of the partial repeats, located at the C terminus of the beta-chain (two helices) and at the N, terminus of the alpha-chain (one helix). This tetramer is the assemblage, able to cross-link actin filaments. Model building by homology of the, "tetramerization" repeat from human erythrocyte spectrin illuminates the, possible role of point mutations which cause hemolytic anemias.
+Cytoskeletal proteins belonging to the spectrin family have an elongated structure composed of repetitive units. The three-dimensional solution structure of the 16th repeat from chicken brain alpha-spectrin (R16) has been determined by NMR spectroscopy and distance geometry-simulated annealing calculations. We used a total of 1035 distance restraints, which included 719 NOE-based values obtained by applying the ambiguous restraints for iterative assignment (ARIA) method. In addition, we performed a direct refinement against 1H-chemical shifts. The final ensemble of 20 structures shows an average RMSD of 1.52 A from the mean for the backbone atoms, excluding loops and N and C termini. R16 is made up of three antiparallel alpha-helices separated by two loops, and folds into a left-handed coiled-coil.The basic unit of spectrin is an antiparallel heterodimer composed of two homologous chains, beta and alpha. These assemble a tetramer via a mechanism that relies on the completion of a single repeat by association of the partial repeats located at the C terminus of the beta-chain (two helices) and at the N terminus of the alpha-chain (one helix). This tetramer is the assemblage able to cross-link actin filaments. Model building by homology of the "tetramerization" repeat from human erythrocyte spectrin illuminates the possible role of point mutations which cause hemolytic anemias.
 ==About this Structure==
-AJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AJ3 OCA].
+AJ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AJ3 OCA].
 ==Reference==
@@ Line 31: / Line 31: @@
 [[Category: spectrin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:53:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:45:02 2008''