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.


1e7n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
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

Image:1e7n.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1e7n"
Personal tools