1bd7
From Proteopedia
(New page: 200px<br /><applet load="1bd7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bd7, resolution 2.78Å" /> '''CIRCULARLY PERMUTED ...) |
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| - | [[Image:1bd7.gif|left|200px]]<br /><applet load="1bd7" size=" | + | [[Image:1bd7.gif|left|200px]]<br /><applet load="1bd7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bd7, resolution 2.78Å" /> | caption="1bd7, resolution 2.78Å" /> | ||
'''CIRCULARLY PERMUTED BB2-CRYSTALLIN'''<br /> | '''CIRCULARLY PERMUTED BB2-CRYSTALLIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The betagamma-crystallins form a superfamily of eye lens proteins | + | The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly. |
==About this Structure== | ==About this Structure== | ||
| - | 1BD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1BD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BD7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Basak, A | + | [[Category: Basak, A K.]] |
[[Category: Glockshuber, R.]] | [[Category: Glockshuber, R.]] | ||
| - | [[Category: Mayr, E | + | [[Category: Mayr, E M.]] |
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: Wright, G.]] | [[Category: Wright, G.]] | ||
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[[Category: multigene family]] | [[Category: multigene family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:02 2008'' |
Revision as of 09:54, 21 February 2008
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CIRCULARLY PERMUTED BB2-CRYSTALLIN
Overview
The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly.
About this Structure
1BD7 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly., Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C, Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330
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