1dsl: Difference between revisions
New page: left|200px<br /><applet load="1dsl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dsl, resolution 1.55Å" /> '''GAMMA B CRYSTALLIN C... |
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[[Image:1dsl.gif|left|200px]]<br /><applet load="1dsl" size=" | [[Image:1dsl.gif|left|200px]]<br /><applet load="1dsl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1dsl, resolution 1.55Å" /> | caption="1dsl, resolution 1.55Å" /> | ||
'''GAMMA B CRYSTALLIN C-TERMINAL DOMAIN'''<br /> | '''GAMMA B CRYSTALLIN C-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
We use protein engineering and crystallography to simulate aspects of the | We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice. | ||
==About this Structure== | ==About this Structure== | ||
1DSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | 1DSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DSL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bateman, O | [[Category: Bateman, O A.]] | ||
[[Category: Driessen, H | [[Category: Driessen, H P.C.]] | ||
[[Category: Glockshuber, R.]] | [[Category: Glockshuber, R.]] | ||
[[Category: Jaenicke, R.]] | [[Category: Jaenicke, R.]] | ||
[[Category: Mayr, E | [[Category: Mayr, E M.]] | ||
[[Category: Norledge, B | [[Category: Norledge, B V.]] | ||
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: eye lens protein]] | [[Category: eye lens protein]] | ||
[[Category: multigene family]] | [[Category: multigene family]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:59 2008'' | ||
Revision as of 13:20, 21 February 2008
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GAMMA B CRYSTALLIN C-TERMINAL DOMAIN
OverviewOverview
We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice.
About this StructureAbout this Structure
1DSL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins., Norledge BV, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HP, Nat Struct Biol. 1996 Mar;3(3):267-74. PMID:8605629
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