1dsl: Difference between revisions
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'''GAMMA B CRYSTALLIN C-TERMINAL DOMAIN''' | '''GAMMA B CRYSTALLIN C-TERMINAL DOMAIN''' | ||
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[[Category: Norledge, B V.]] | [[Category: Norledge, B V.]] | ||
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: | [[Category: Eye lens protein]] | ||
[[Category: | [[Category: Multigene family]] | ||
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Revision as of 14:13, 2 May 2008
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 Page seeded by OCA on Fri May 2 14:13:26 2008