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.


2gbv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gbv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2gbv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gbv| PDB=2gbv | SCENE= }}
{{STRUCTURE_2gbv| PDB=2gbv | SCENE= }}
-
'''C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase'''
+
===C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase===
-
==Overview==
+
<!--
-
The gain of neurotoxic function in amyotrophic lateral sclerosis (ALS) has been linked to misfolding of the homodimeric enzyme Cu/Zn superoxide dismutase (SOD). Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. A hallmark of this species is that it fails to dimerize and becomes trapped as a monomer in the absence of the active-site metals. The crystallographic data show that removal of the C57-C146 disulphide bond sets free the interface loop IV in the apo protein, whereas the same loop remains unaffected in the holo protein. Thus, the low dimerisation propensity of disulphide-reduced apoSOD seems to be of entropic origin due to increased loop flexibility in the monomeric state: in the disulphide-reduced holo protein this gain in configurational entropy upon splitting of the dimer interface is reduced by the metal coordination.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17070542}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17070542 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17070542}}
==Disease==
==Disease==
Line 33: Line 37:
[[Category: Human cu/zn superoxide dismutase]]
[[Category: Human cu/zn superoxide dismutase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:55:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:12:33 2008''

Revision as of 18:12, 28 July 2008

Image:2gbv.png

Template:STRUCTURE 2gbv

Contents

C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase

Template:ABSTRACT PUBMED 17070542

Disease

Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]

About this Structure

2GBV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase., Hornberg A, Logan DT, Marklund SL, Oliveberg M, J Mol Biol. 2007 Jan 12;365(2):333-42. Epub 2006 Sep 23. PMID:17070542

Page seeded by OCA on Mon Jul 28 21:12:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gbv"
Personal tools