1b3u: Difference between revisions
New page: left|200px<br /> <applet load="1b3u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b3u, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1b3u.gif|left|200px]]<br /> | [[Image:1b3u.gif|left|200px]]<br /><applet load="1b3u" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1b3u, resolution 2.3Å" /> | caption="1b3u, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA'''<br /> | '''CRYSTAL STRUCTURE OF CONSTANT REGULATORY DOMAIN OF HUMAN PP2A, PR65ALPHA'''<br /> | ||
==Overview== | ==Overview== | ||
The PR65/A subunit of protein phosphatase 2A serves as a scaffolding | 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== | ||
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:// | 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.]] | ||
[[Category: Groves, M | [[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]] | ||
''Page seeded by [http:// | ''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
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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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