1ha4
From Proteopedia
(New page: 200px<br /> <applet load="1ha4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ha4, resolution 2.4Å" /> '''GAMMAS CRYSTALLIN C ...) |
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| - | [[Image:1ha4.gif|left|200px]]<br /> | + | [[Image:1ha4.gif|left|200px]]<br /><applet load="1ha4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ha4" size=" | + | |
caption="1ha4, resolution 2.4Å" /> | caption="1ha4, resolution 2.4Å" /> | ||
'''GAMMAS CRYSTALLIN C TERMINAL DOMAIN FROM HOMO SAPIENS'''<br /> | '''GAMMAS CRYSTALLIN C TERMINAL DOMAIN FROM HOMO SAPIENS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | gammaS-crystallin is a major human lens protein found in the outer region | + | gammaS-crystallin is a major human lens protein found in the outer region of the eye lens, where the refractive index is low. Because crystallins are not renewed they acquire post-translational modifications that may perturb stability and solubility. In common with other members of the betagamma-crystallin superfamily, gammaS-crystallin comprises two similar beta-sheet domains. The crystal structure of the C-terminal domain of human gammaS-crystallin has been solved at 2.4 A resolution. The structure shows that in the in vitro expressed protein, the buried cysteines remain reduced. The backbone conformation of the "tyrosine corner" differs from that of other betagamma-crystallins because of deviation from the consensus sequence. The two C-terminal domains in the asymmetric unit are organized about a slightly distorted 2-fold axis to form a dimer with similar geometry to full-length two-domain family members. Two glutamines found in lattice contacts may be important for short range interactions in the lens. An asparagine known to be deamidated in human cataract is located in a highly ordered structural region. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1HA4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HA4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bateman, O | + | [[Category: Bateman, O A.]] |
| - | [[Category: Goodfellow, J | + | [[Category: Goodfellow, J M.]] |
| - | [[Category: Purkiss, A | + | [[Category: Purkiss, A G.]] |
[[Category: Slingsby, C.]] | [[Category: Slingsby, C.]] | ||
[[Category: eye lens protein]] | [[Category: eye lens protein]] | ||
[[Category: gammas crystallin]] | [[Category: gammas crystallin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:08 2008'' |
Revision as of 10:59, 21 February 2008
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GAMMAS CRYSTALLIN C TERMINAL DOMAIN FROM HOMO SAPIENS
Contents |
Overview
gammaS-crystallin is a major human lens protein found in the outer region of the eye lens, where the refractive index is low. Because crystallins are not renewed they acquire post-translational modifications that may perturb stability and solubility. In common with other members of the betagamma-crystallin superfamily, gammaS-crystallin comprises two similar beta-sheet domains. The crystal structure of the C-terminal domain of human gammaS-crystallin has been solved at 2.4 A resolution. The structure shows that in the in vitro expressed protein, the buried cysteines remain reduced. The backbone conformation of the "tyrosine corner" differs from that of other betagamma-crystallins because of deviation from the consensus sequence. The two C-terminal domains in the asymmetric unit are organized about a slightly distorted 2-fold axis to form a dimer with similar geometry to full-length two-domain family members. Two glutamines found in lattice contacts may be important for short range interactions in the lens. An asparagine known to be deamidated in human cataract is located in a highly ordered structural region.
Disease
Known disease associated with this structure: Cataract, progressive polymorphic cortical OMIM:[123730]
About this Structure
1HA4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The X-ray crystal structure of human gamma S-crystallin C-terminal domain., Purkiss AG, Bateman OA, Goodfellow JM, Lubsen NH, Slingsby C, J Biol Chem. 2002 Feb 8;277(6):4199-205. Epub 2001 Nov 8. PMID:11706012
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