1dsl
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(New page: 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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Revision as of 11:25, 20 November 2007
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GAMMA B CRYSTALLIN C-TERMINAL DOMAIN
Overview
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
1DSL is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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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