1s35

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(New page: 200px<br /> <applet load="1s35" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s35, resolution 2.40&Aring;" /> '''Crystal Structure o...)
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<applet load="1s35" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1s35, resolution 2.40&Aring;" />
caption="1s35, resolution 2.40&Aring;" />
'''Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin'''<br />
'''Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin'''<br />
==Overview==
==Overview==
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Erythroid spectrin, a major component of the cytoskeletal network of the, red cell which contributes to both the stability and the elasticity of the, red cell membrane, is composed of two subunits, alpha and beta, each, formed by 16-20 tandem repeats. The properties of the repeats and their, relative arrangement are thought to be key determinants of spectrin, flexibility. Here we report a 2.4 A resolution crystal structure of human, erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is, unusual as it exhibits low stability of folding and one of its repeats, lacks two tryptophans highly conserved among spectrin repeats. Two key, factors responsible for the lower stability and, possibly, its, flexibility, are revealed by the structure. A third novel feature of the, structure is the relative orientation of the two repeats, which increases, the range of possible conformations and provides new insights into atomic, models of spectrin flexibility.
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Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1S35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S35 OCA].
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1S35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S35 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kusunoki, H.]]
[[Category: Kusunoki, H.]]
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[[Category: MacDonald, R.I.]]
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[[Category: MacDonald, R I.]]
[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: two repeats of spectrin]]
[[Category: two repeats of spectrin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:09:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:23 2008''

Revision as of 12:57, 21 February 2008


1s35, resolution 2.40Å

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Crystal Structure of Repeats 8 and 9 of Human Erythroid Spectrin

Contents

Overview

Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it exhibits low stability of folding and one of its repeats lacks two tryptophans highly conserved among spectrin repeats. Two key factors responsible for the lower stability and, possibly, its flexibility, are revealed by the structure. A third novel feature of the structure is the relative orientation of the two repeats, which increases the range of possible conformations and provides new insights into atomic models of spectrin flexibility.

Disease

Known diseases associated with this structure: Anemia, neonatal hemolytic, fatal and near-fatal OMIM:[182870], Elliptocytosis-3 OMIM:[182870], Spherocytosis-1 OMIM:[182870]

About this Structure

1S35 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural insights into the stability and flexibility of unusual erythroid spectrin repeats., Kusunoki H, MacDonald RI, Mondragon A, Structure. 2004 Apr;12(4):645-56. PMID:15062087

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