1ttc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ttc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ttc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ttc| PDB=1ttc | SCENE= }}
{{STRUCTURE_1ttc| PDB=1ttc | SCENE= }}
-
'''THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION'''
+
===THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The x-ray crystal structures of normal human transthyretin (prealbumin) and the amyloidogenic Val-30-Met variant have been refined at 1.7-A resolution to R-values of 0.168 and 0.179, respectively, for 19,882 and 20,362 reflections (Fobs &gt; 2.0 sigma). Standard deviations for stereochemical parameters are 0.018 and 0.022 A for bond distances, 0.030 and 0.038 A for angle distances, and 0.035 and 0.070 A for planar 1-4 distances. The newly refined normal structure shows improvement over the original structure of Blake and Swan (Blake, C. C. F., and Swan, I. D. A. (1971) J. Mol. Biol. 61, 217-224) in stereochemistry and in the conformation of the loop regions. Residues Arg-103, Thr-123, Asn-124, and Pro-125 have now been resolved, and residues 1-9 and 126-127 have been modeled with the aid of simulated annealing refinement. The functional form of transthyretin is a tetramer, having a cylindrical cavity which will bind thyroxine and an exterior binding site for the complex of retinol with retinol-binding protein. The monomer is a beta barrel flattened to become more like a sandwich with residue 30 in the interior. The methionyl for valyl substitution forces the beta sheets of the monomer as much as 1 A apart, resulting in a distortion of the thyroxine-binding cavity, in agreement with the independent observations that the Met-30 variant has low affinity for thyroxine.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8428915}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8428915 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8428915}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Hamilton, J A.]]
[[Category: Hamilton, J A.]]
[[Category: Steinrauf, L K.]]
[[Category: Steinrauf, L K.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:20:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:50:01 2008''

Revision as of 17:50, 27 July 2008

Image:1ttc.png

Template:STRUCTURE 1ttc

THE X-RAY CRYSTAL STRUCTURE REFINEMENTS OF NORMAL HUMAN TRANSTHYRETIN AND THE AMYLOIDOGENIC VAL30MET VARIANT TO 1.7 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8428915

About this Structure

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

Reference

The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30-->Met variant to 1.7-A resolution., Hamilton JA, Steinrauf LK, Braden BC, Liepnieks J, Benson MD, Holmgren G, Sandgren O, Steen L, J Biol Chem. 1993 Feb 5;268(4):2416-24. PMID:8428915

Page seeded by OCA on Sun Jul 27 20:50:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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