1bd7

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[[Image:1bd7.gif|left|200px]]<br /><applet load="1bd7" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bd7.gif|left|200px]]
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caption="1bd7, resolution 2.78&Aring;" />
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'''CIRCULARLY PERMUTED BB2-CRYSTALLIN'''<br />
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{{Structure
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|PDB= 1bd7 |SIZE=350|CAPTION= <scene name='initialview01'>1bd7</scene>, resolution 2.78&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''CIRCULARLY PERMUTED BB2-CRYSTALLIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1BD7 is a [[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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9655330 9655330]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9655330 9655330]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: multigene family]]
[[Category: multigene family]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:25 2008''

Revision as of 08:09, 20 March 2008

Image:1bd7.gif


PDB ID 1bd7

Drag the structure with the mouse to rotate
, resolution 2.78Å
Coordinates: save as pdb, mmCIF, xml



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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