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.


1izb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1izb.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1izb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1izb| PDB=1izb | SCENE= }}
{{STRUCTURE_1izb| PDB=1izb | SCENE= }}
-
'''ROLE OF B13 GLU IN INSULIN ASSEMBLY: THE HEXAMER STRUCTURE OF RECOMBINANT MUTANT (B13 GLU-> GLN) INSULIN'''
+
===ROLE OF B13 GLU IN INSULIN ASSEMBLY: THE HEXAMER STRUCTURE OF RECOMBINANT MUTANT (B13 GLU-> GLN) INSULIN===
-
==Overview==
+
<!--
-
The assembly of the insulin hexamer brings the six B13 glutamate side-chains at the centre into close proximity. Their mutual repulsion is unfavourable and zinc co-ordination to B10 histidine is necessary to stabilize the well known zinc-containing hexamers. Since B13 is always a carboxylic acid in all known sequences of hexamer forming insulins, it is likely to be important in the hormone's biology. The mutation of B13 Glu--&gt;Gln leads to a stable zinc-free hexamer with somewhat reduced potency. The structures of the zinc-free B13 Gln hexamer and the 2Zn B13 insulin hexamer have been determined by X-ray analysis and refined with 2.5 A and 2.0 A diffraction data, respectively. Comparisons show that in 2Zn B13 Gln insulin, the hexamer structure (T6) is very like that of the native hormone. On the other hand, the zinc-free hexamer assumes a quaternary structure (T3/R3) seen in the native 4Zn insulin hexamer, and normally associated only with high chloride ion concentrations in the medium. The crystal structures show the B13 Gln side-chains only contact water in contrast to the B13 glutamate in 2Zn insulin. The solvation of the B13 Gln may be associated with this residue favouring helix at B1 to B8. The low potency of the B13 Gln insulin also suggests the residue influences the hormone's conformation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1361949}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1361949 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1361949}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Xiao, B.]]
[[Category: Xiao, B.]]
[[Category: Hormone]]
[[Category: Hormone]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:36:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:15:48 2008''

Revision as of 11:15, 1 July 2008

Image:1izb.png

Template:STRUCTURE 1izb

ROLE OF B13 GLU IN INSULIN ASSEMBLY: THE HEXAMER STRUCTURE OF RECOMBINANT MUTANT (B13 GLU-> GLN) INSULIN

Template:ABSTRACT PUBMED 1361949

About this Structure

1IZB is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Role of B13 Glu in insulin assembly. The hexamer structure of recombinant mutant (B13 Glu-->Gln) insulin., Bentley GA, Brange J, Derewenda Z, Dodson EJ, Dodson GG, Markussen J, Wilkinson AJ, Wollmer A, Xiao B, J Mol Biol. 1992 Dec 20;228(4):1163-76. PMID:1361949

Page seeded by OCA on Tue Jul 1 14:15:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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