This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1h4a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h4a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1h4a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h4a| PDB=1h4a | SCENE= }}
{{STRUCTURE_1h4a| PDB=1h4a | SCENE= }}
-
'''HUMAN GAMMA-D CRYSTALLIN R58H MUTANT STRUCTURE AT 1.15 A RESOLUTION'''
+
===HUMAN GAMMA-D CRYSTALLIN R58H MUTANT STRUCTURE AT 1.15 A RESOLUTION===
-
==Overview==
+
<!--
-
Several human cataracts have been linked to mutations in the gamma crystallin gene. One of these is the aculeiform cataract, which is caused by an R58H mutation in gammaD crystallin. We have shown previously that this cataract is caused by crystallization of the mutant protein, which is an order of magnitude less soluble than the wild-type. Here, we report the very high-resolution crystal structures of the mutant and wild-type proteins. Both proteins crystallize in the same space group and lattice. Thus, a strict comparison of the protein-protein and protein-water intermolecular interactions in the two crystal lattices is possible. Overall, the differences between the mutant and wild-type structures are small. At position 58, the mutant protein loses the direct ion-pair intermolecular interaction present in the wild-type, due to the differences between histidine and arginine at the atomic level; the interaction in the mutant is mediated by water molecules. Away from the mutation site, the mutant and wild-type lattice structures differ in the identity of side-chains that occupy alternate conformations. Since the interactions in the crystal phase are very similar for the two proteins, we conclude that the reduction in the solubility of the mutant is mainly due to the effect of the R58H mutation in the solution phase. The results presented here are also important as they are the first high-resolution X-ray structures of human gamma crystallins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12729747}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12729747 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12729747}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Crystallin]]
[[Category: Crystallin]]
[[Category: Eye lens protein]]
[[Category: Eye lens protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:24:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:35:59 2008''

Revision as of 03:36, 1 July 2008

Image:1h4a.png

Template:STRUCTURE 1h4a

HUMAN GAMMA-D CRYSTALLIN R58H MUTANT STRUCTURE AT 1.15 A RESOLUTION

Template:ABSTRACT PUBMED 12729747

About this Structure

1H4A is a Single protein structure. Full crystallographic information is available from OCA.

Reference

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract., Basak A, Bateman O, Slingsby C, Pande A, Asherie N, Ogun O, Benedek GB, Pande J, J Mol Biol. 2003 May 16;328(5):1137-47. PMID:12729747

Page seeded by OCA on Tue Jul 1 06:35:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h4a"
Personal tools