1e7n

<table><tr><td colspan='2'>[[1e7n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7N FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7n OCA], [https://pdbe.org/1e7n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7n RCSB], [https://www.ebi.ac.uk/pdbsum/1e7n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7n ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/CRBB2_MOUSE CRBB2_MOUSE]] Crystallins are the dominant structural components of the vertebrate eye lens.

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== Publication Abstract from PubMed ==

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 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<ref>PMID:11090271</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Lk3 transgenic mice]]

[[Category: Basak, A]]

[[Category: Bateman, O A]]

[[Category: Clout, N J]]

[[Category: Jaenicke, R]]

[[Category: Slingsby, C]]

[[Category: Wieligmann, K]]

[[Category: Structural protein]]