1dsl
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsl OCA], [http://www.ebi.ac.uk/pdbsum/1dsl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dsl RCSB]</span> | ||
}} | }} | ||
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[[Category: multigene family]] | [[Category: multigene family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:51 2008'' |
Revision as of 16:48, 30 March 2008
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| , resolution 1.55Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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