From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1e7n.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1e7n.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1e7n| PDB=1e7n | SCENE= }} | | {{STRUCTURE_1e7n| PDB=1e7n | SCENE= }} |
| | | | |
| - | '''THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER'''
| + | ===THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | betagamma-crystallins from the eye lens are proteins consisting of two similar domains joined by a short linker. All three-dimensional structures of native proteins solved so far reveal similar pseudo-2-fold pairing of the domains reflecting their presumed ancient origin from a single-domain homodimer. However, studies of engineered single domains of members of the betagamma-crystallin superfamily have not revealed a prototype ancestral solution homodimer. Here we report the 2.35 A X-ray structure of the homodimer of the N-terminal domain of rat betaB2-crystallin (betaB2-N). The two identical domains pair in a symmetrical manner very similar to that observed in native betagamma-crystallins, where N and C-terminal domains (which share approximately 35% sequence identity) are related by a pseudo-2-fold axis. betaB2-N thus resembles the ancestral prototype of the betagamma-crystallin superfamily as it self-associates in solution to form a dimer with an essentially identical domain interface as that between the N and C domains in betagamma-crystallins, but without the benefit of a covalent linker. The structure provides further evidence for the role of two-domain pairing in stabilising the protomer fold. These results support the view that the betagamma-crystallin superfamily has evolved by a series of gene duplication and fusion events from a single-domain ancestor capable of forming homodimers.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11090271}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11090271 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11090271}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Eye lens]] | | [[Category: Eye lens]] |
| | [[Category: Protein structure]] | | [[Category: Protein structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:45:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:17:05 2008'' |
Revision as of 21:17, 30 June 2008
Template:STRUCTURE 1e7n
THE N-TERMINAL DOMAIN OF BETA-B2-CRYSTALLIN RESEMBLES THE PUTATIVE ANCESTRAL HOMODIMER
Template:ABSTRACT PUBMED 11090271
About this Structure
1E7N is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer., Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C, J Mol Biol. 2000 Dec 1;304(3):253-7. PMID:11090271
Page seeded by OCA on Tue Jul 1 00:17:05 2008
