1b3u

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(New page: 200px<br /> <applet load="1b3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b3u, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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caption="1b3u, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA'''<br />
'''CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA'''<br />
==Overview==
==Overview==
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The PR65/A subunit of protein phosphatase 2A serves as a scaffolding, molecule to coordinate the assembly of the catalytic subunit and a, variable regulatory B subunit, generating functionally diverse, heterotrimers. Mutations of the beta isoform of PR65 are associated with, lung and colon tumors. The crystal structure of the PR65/Aalpha subunit, at 2.3 A resolution, reveals the conformation of its 15 tandemly repeated, HEAT sequences, degenerate motifs of approximately 39 amino acids present, in a variety of proteins, including huntingtin and importin beta., Individual motifs are composed of a pair of antiparallel alpha helices, that assemble in a mainly linear, repetitive fashion to form an elongated, molecule characterized by a double layer of alpha helices. Left-handed, rotations at three interrepeat interfaces generate a novel left-hand, superhelical conformation. The protein interaction interface is formed, from the intrarepeat turns that are aligned to form a continuous ridge.
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The PR65/A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit, generating functionally diverse heterotrimers. Mutations of the beta isoform of PR65 are associated with lung and colon tumors. The crystal structure of the PR65/Aalpha subunit, at 2.3 A resolution, reveals the conformation of its 15 tandemly repeated HEAT sequences, degenerate motifs of approximately 39 amino acids present in a variety of proteins, including huntingtin and importin beta. Individual motifs are composed of a pair of antiparallel alpha helices that assemble in a mainly linear, repetitive fashion to form an elongated molecule characterized by a double layer of alpha helices. Left-handed rotations at three interrepeat interfaces generate a novel left-hand superhelical conformation. The protein interaction interface is formed from the intrarepeat turns that are aligned to form a continuous ridge.
==About this Structure==
==About this Structure==
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1B3U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B3U OCA].
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1B3U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3U OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barford, D.]]
[[Category: Barford, D.]]
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[[Category: Groves, M.R.]]
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[[Category: Groves, M R.]]
[[Category: Hanlon, N.]]
[[Category: Hanlon, N.]]
[[Category: Hemmings, B.]]
[[Category: Hemmings, B.]]
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[[Category: scaffold protein]]
[[Category: scaffold protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:09 2008''

Revision as of 09:51, 21 February 2008


1b3u, resolution 2.3Å

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CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA

Overview

The PR65/A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit, generating functionally diverse heterotrimers. Mutations of the beta isoform of PR65 are associated with lung and colon tumors. The crystal structure of the PR65/Aalpha subunit, at 2.3 A resolution, reveals the conformation of its 15 tandemly repeated HEAT sequences, degenerate motifs of approximately 39 amino acids present in a variety of proteins, including huntingtin and importin beta. Individual motifs are composed of a pair of antiparallel alpha helices that assemble in a mainly linear, repetitive fashion to form an elongated molecule characterized by a double layer of alpha helices. Left-handed rotations at three interrepeat interfaces generate a novel left-hand superhelical conformation. The protein interaction interface is formed from the intrarepeat turns that are aligned to form a continuous ridge.

About this Structure

1B3U is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs., Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D, Cell. 1999 Jan 8;96(1):99-110. PMID:9989501

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