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1gam
From Proteopedia
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| - | [[Image:1gam.jpg|left|200px]] | + | [[Image:1gam.jpg|left|200px]] |
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| - | '''GAMMA B CRYSTALLIN TRUNCATED C-TERMINAL DOMAIN''' | + | {{Structure |
| + | |PDB= 1gam |SIZE=350|CAPTION= <scene name='initialview01'>1gam</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GAMMA B CRYSTALLIN TRUNCATED C-TERMINAL DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GAM is a [ | + | 1GAM is a [[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=1GAM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8605629 8605629] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: multigene family]] | [[Category: multigene family]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:44 2008'' |
Revision as of 09:20, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GAMMA B CRYSTALLIN TRUNCATED 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
1GAM 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
Page seeded by OCA on Thu Mar 20 11:20:44 2008
