2spc

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{{STRUCTURE_2spc| PDB=2spc | SCENE= }}
{{STRUCTURE_2spc| PDB=2spc | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN'''
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===CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN===
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==Overview==
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The elongated proteins of the spectrin family (dystrophin, alpha-actinin, and spectrin) contain tandemly repeated segments and form resilient cellular meshworks by cross-linking actin filaments. The structure of one of the repetitive segments of alpha-spectrin was determined at a 1.8 angstrom resolution. A segment consists of a three-helix bundle. A model of the interface between two tandem segments suggests that hydrophobic interactions between segments may constrain intersegment flexibility. The helix side chain interactions explain how mutations that are known to produce hemolytic anemias disrupt spectrin associations that sustain the integrity of the erythrocyte membrane.
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{{ABSTRACT_PUBMED_8266097}}
==About this Structure==
==About this Structure==
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[[Category: Yan, Y.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:44:01 2008''

Revision as of 19:44, 27 July 2008

Template:STRUCTURE 2spc

CRYSTAL STRUCTURE OF THE REPETITIVE SEGMENTS OF SPECTRIN

Template:ABSTRACT PUBMED 8266097

About this Structure

2SPC is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Crystal structure of the repetitive segments of spectrin., Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D, Science. 1993 Dec 24;262(5142):2027-30. PMID:8266097

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