1tt6: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1tt6.gif|left|200px]]
{{Seed}}
[[Image:1tt6.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tt6|  PDB=1tt6  |  SCENE=  }}  
{{STRUCTURE_1tt6|  PDB=1tt6  |  SCENE=  }}  


'''The orthorhombic crystal structure of transthyretin in complex with diethylstilbestrol'''
===The orthorhombic crystal structure of transthyretin in complex with diethylstilbestrol===




==Overview==
<!--
Transthyretin (TTR) is a homotetrameric plasma protein that, in conditions not yet completely understood, may aggregate, forming the fibrillar material associated with TTR amyloidosis. A number of reported experiments indicate that dissociation of the TTR tetramer occurs prior to fibril formation, and therefore, studies aiming at the discovery of compounds that stabilize the protein quaternary structure, thereby acting as amyloid inhibitors, are being performed. The ability of diethylstilbestrol (DES) to act as a competitive inhibitor for the thyroid hormone binding to TTR indicated a possible stabilizing effect of DES upon binding. Here we report the crystallographic study of DES binding to TTR. The structural data reveal two different binding modes, both located in the thyroxine binding channel. In both cases, DES binds deeply in the channel and establishes interactions with the equivalent molecule present in the adjacent binding site. The most remarkable features of DES interaction with TTR are its hydrophobic interactions within the protein halogen binding pockets, where its ethyl groups are snugly fitted, and the hydrogen bonds established at the center of the tetramer with Ser-117. Experiments concerning amyloid formation in vitro suggest that DES is effectively an amyloid inhibitor in acid-mediated fibrillogenesis and may be used for the design of more powerful drugs. The present study gave us further insight in the molecular mechanism by which DES competes with thyroid hormone binding to TTR and highlights key interactions between DES and TTR that oppose amyloid formation.
The line below this paragraph, {{ABSTRACT_PUBMED_15469931}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15469931 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15469931}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Protein stabilization]]
[[Category: Protein stabilization]]
[[Category: Transthyretin]]
[[Category: Transthyretin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:19:59 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:28:48 2008''

Revision as of 06:28, 28 July 2008

File:1tt6.png

Template:STRUCTURE 1tt6

The orthorhombic crystal structure of transthyretin in complex with diethylstilbestrol

Template:ABSTRACT PUBMED 15469931

About this Structure

1TT6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of transthyretin in complex with diethylstilbestrol: a promising template for the design of amyloid inhibitors., Morais-de-Sa E, Pereira PJ, Saraiva MJ, Damas AM, J Biol Chem. 2004 Dec 17;279(51):53483-90. Epub 2004 Oct 6. PMID:15469931

Page seeded by OCA on Mon Jul 28 09:28:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1tt6&oldid=692130"