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.


1ben

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ben.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ben.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ben| PDB=1ben | SCENE= }}
{{STRUCTURE_1ben| PDB=1ben | SCENE= }}
-
'''INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE'''
+
===INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE===
-
==Overview==
+
<!--
-
The structure of a symmetric T3R3f insulin hexamer, complexed with 4-hydroxybenzamide, has been determined using X-ray crystallographic techniques. Data were measured from six crystals grown in microgravity to a resolution of 1.4 A and the structure has been refined including the contributions from hydrogen atoms. The crystals are isomorphous with T3R3f complexes of phenolic derivatives as well as with uncomplexed forms. Unlike the structures of complexes with phenol, m-cresol, resorcinol, 4'-hydroxyacetanilide, and methylparaben, which bind one phenolic derivative molecule per R- or Rf-state monomer, two molecules of 4-hydroxybenzamide are bound by each Rf-state monomer. The presence of the second guest molecule results in an extensive hydrogen bonding network, mediated by water molecules, between the T- and Rf-state trimers and adds stability to the formation of the hexamer. The only access to these second sites is through three symmetry-related, narrow channels that originate on the surface of the T-state trimer. Although the conformation of the backbone atoms of the monomers is nearly identical to that of other T3R3f hexamers, significant changes are observed in the conformations of side chains in the vicinity of the second binding site. The side chain of the T-state A11 Cys residue, which forms a disulfide bond to A6 Cys in the same monomer, is observed in two discrete conformations; two discrete conformations are also present for the entire A8 Thr residue in the Rf-state monomer. A procedure is also described for an alternate method of interframe scaling and merging intensity data from an image plate detector.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8844841}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8844841 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8844841}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Hormone]]
[[Category: Hormone]]
[[Category: Insulin]]
[[Category: Insulin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:25:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:59:27 2008''

Revision as of 15:59, 30 June 2008

Image:1ben.png

Template:STRUCTURE 1ben

INSULIN COMPLEXED WITH 4-HYDROXYBENZAMIDE

Template:ABSTRACT PUBMED 8844841

About this Structure

1BEN is a Protein complex structure. Full crystallographic information is available from OCA.

Reference

A novel complex of a phenolic derivative with insulin: structural features related to the T-->R transition., Smith GD, Ciszak E, Pangborn W, Protein Sci. 1996 Aug;5(8):1502-11. PMID:8844841

Page seeded by OCA on Mon Jun 30 18:59:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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