5ttr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:5ttr.gif|left|200px]]
[[Image:5ttr.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 5ttr |SIZE=350|CAPTION= <scene name='initialview01'>5ttr</scene>, resolution 2.7&Aring;
+
The line below this paragraph, containing "STRUCTURE_5ttr", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_5ttr| PDB=5ttr | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ttr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttr OCA], [http://www.ebi.ac.uk/pdbsum/5ttr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=5ttr RCSB]</span>
+
-
}}
+
'''LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE'''
'''LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE'''
Line 28: Line 25:
[[Category: Saraiva, M J.]]
[[Category: Saraiva, M J.]]
[[Category: Sebastiao, M P.]]
[[Category: Sebastiao, M P.]]
-
[[Category: amyloid]]
+
[[Category: Amyloid]]
-
[[Category: crystal structure]]
+
[[Category: Crystal structure]]
-
[[Category: fap]]
+
[[Category: Fap]]
-
[[Category: thyroxine]]
+
[[Category: Thyroxine]]
-
[[Category: transport]]
+
[[Category: Transport]]
-
[[Category: transthyretin]]
+
[[Category: Transthyretin]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:38:19 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:42:23 2008''
+

Revision as of 19:38, 4 May 2008

Template:STRUCTURE 5ttr

LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE


Overview

The x-ray crystal structure of the amyloidogenic Leu55 --> Pro transthyretin (TTR) variant, implicated as the causative agent in early-onset familial amyloidotic polyneuropathy (Jacobson, D. R., McFarlin, D. E., Kane, I., and Buxbaum, J. N. (1992) Hum. Genet. 89, 353-356), has been solved by molecular replacement, refined at 2.7 A to a Rcryst value of 0.190 (Fobs > 2.0sigma), and compared with wild-type transthyretin to understand the molecular mechanism(s) involved in amyloidogenesis. Leu55 --> Pro TTR crystallizes in space group C2, with eight monomers in the asymmetric unit, and the observed packing contacts are considerably different from those described for the wild-type protein. Refinement of the crystal structure shows that the proline for leucine substitution disrupts the hydrogen bonds between strands D and A, resulting in different interface contacts. Based on the assumption that the observed packing contacts may be significant for amyloidogenesis, a model for the TTR amyloid is proposed. It consists of a tubular structure with inner and outer diameters approximately of 30 and 100 A and four monomers per cross-section.

About this Structure

5TTR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils., Sebastiao MP, Saraiva MJ, Damas AM, J Biol Chem. 1998 Sep 18;273(38):24715-22. PMID:9733771 Page seeded by OCA on Sun May 4 22:38:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools