2bv2
From Proteopedia
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BETA GAMMA CRYSTALLIN FROM CIONA INTESTINALIS
Overview
A refracting lens is a key component of our image-forming camera eye;, however, its evolutionary origin is unknown because precursor structures, appear absent in nonvertebrates. The vertebrate betagamma-crystallin genes, encode abundant structural proteins critical for the function of the lens., We show that the urochordate Ciona intestinalis, which split from the, vertebrate lineage before the evolution of the lens, has a single gene, coding for a single domain monomeric betagamma-crystallin. The crystal, structure of Ciona betagamma-crystallin is very similar to that of a, vertebrate betagamma-crystallin domain, except for paired, occupied, calcium binding sites. The Ciona betagamma-crystallin is only expressed in, the palps and in the otolith, the pigmented sister cell of the, ... [(full description)]
About this Structure
2BV2 is a [Single protein] structure of sequence from [Ciona intestinalis] with CA, ACT and SO4 as [ligands]. Full crystallographic information is available from [OCA].
Reference
Urochordate betagamma-crystallin and the evolutionary origin of the vertebrate eye lens., Shimeld SM, Purkiss AG, Dirks RP, Bateman OA, Slingsby C, Lubsen NH, Curr Biol. 2005 Sep 20;15(18):1684-9. PMID:16169492
Page seeded by OCA on Mon Oct 29 20:04:51 2007
Categories: Ciona intestinalis | Single protein | Bateman, O.A. | Dirks, R.P.H. | Lubsen, N.H. | Purkiss, A.G. | Shimeld, S.M. | Slingsby, C. | ACT | CA | SO4 | Ascidian | Calcium binding | Chordate | Crystallin | Eye lens | Spherulin
