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.


1o70

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o70.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1o70.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o70| PDB=1o70 | SCENE= }}
{{STRUCTURE_1o70| PDB=1o70 | SCENE= }}
-
'''NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I'''
+
===NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I===
-
==Overview==
+
<!--
-
Fasciclin I is an insect neural cell adhesion molecule consisting of four FAS1 domains, homologs of which are present in many bacterial, plant, and animal proteins. The crystal structure of FAS1 domains 3 and 4 of Drosophila fasciclin I reveals a novel domain fold, consisting of a seven-stranded beta wedge and a number of alpha helices. The two domains are arranged in a linear fashion and interact through a substantial polar interface. Missense mutations in the FAS1 domains of the human protein betaig-h3 cause corneal dystrophies. Many mutations alter highly conserved core residues, but the two most common mutations, affecting Arg-124 and Arg-555, map to exposed alpha-helical regions, suggesting reduced protein solubility as the disease mechanism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12575939}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12575939 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12575939}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Extracellular module]]
[[Category: Extracellular module]]
[[Category: Genetic disorder]]
[[Category: Genetic disorder]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:27:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:59:08 2008''

Revision as of 13:59, 28 July 2008

Template:STRUCTURE 1o70

NOVEL FOLD REVEALED BY THE STRUCTURE OF A FAS1 DOMAIN PAIR FROM THE INSECT CELL ADHESION MOLECULE FASCICLIN I

Template:ABSTRACT PUBMED 12575939

About this Structure

1O70 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I., Clout NJ, Tisi D, Hohenester E, Structure. 2003 Feb;11(2):197-203. PMID:12575939

Page seeded by OCA on Mon Jul 28 16:59:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools