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.


1vig

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE= HUMAN VIGILIN SIXTH KH REPEAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= HUMAN VIGILIN SIXTH KH REPEAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1vih|1VIH]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vig OCA], [http://www.ebi.ac.uk/pdbsum/1vig PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vig RCSB]</span>
}}
}}
Line 31: Line 34:
[[Category: rna-binding protein]]
[[Category: rna-binding protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:01 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:54 2008''

Revision as of 21:24, 30 March 2008


PDB ID 1vig

Drag the structure with the mouse to rotate
Gene: HUMAN VIGILIN SIXTH KH REPEAT (Homo sapiens)
Related: 1VIH


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



NMR STUDY OF VIGILIN, REPEAT 6, 40 STRUCTURES


Overview

The KH module is a sequence motif found in a number of proteins that are known to be in close association with RNA. Experimental evidence suggests a direct involvement of KH in RNA binding. The human FMR1 protein, which has two KH domains, is associated with fragile X syndrome, the most common inherited cause of mental retardation. Here we present the three-dimensional solution structure of the KH module. The domain consists of a stable beta alpha alpha beta beta alpha fold. On the basis of our results, we suggest a potential surface for RNA binding centered on the loop between the first two helices. Substitution of a well-conserved hydrophobic residue located on the second helix destroys the KH fold; a mutation of this position in FMR1 leads to an aggravated fragile X phenotype.

About this Structure

1VIG is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome., Musco G, Stier G, Joseph C, Castiglione Morelli MA, Nilges M, Gibson TJ, Pastore A, Cell. 1996 Apr 19;85(2):237-45. PMID:8612276

Page seeded by OCA on Mon Mar 31 00:24:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools