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.


1hut

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hut.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hut.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hut| PDB=1hut | SCENE= }}
{{STRUCTURE_1hut| PDB=1hut | SCENE= }}
-
'''THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER'''
+
===THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER===
-
==Overview==
+
<!--
-
The structure of a complex between human alpha-thrombin and a GGTTGGTGTGGTTGG 15-nucleotide consensus sequence has been solved by x-ray crystallography and refined at 2.9-A resolution to an R value of 0.159. As in solution, in the complex the single-stranded DNA folds into a structure with two G-quartets. The DNA is sandwiched between two different positively charged regions of two symmetry-related thrombin molecules in the crystal structure making ionic and hydrophobic interactions. One region is the fibrinogen recognition exosite and the other, the putative heparin binding site. The lack of inhibition of fibrinogen clotting and platelet activation by the DNA 15-mer with the Arg75--&gt;Glu mutant of thrombin is consistent with the several salt bridges of the DNA in the fibrinogen exosite. The association of DNA with the heparin site of a neighboring molecule appears to simply compensate residual charge. Differences in the 15-mer loop conformations between the complex and NMR solution structures can be attributed to conformational changes upon thrombin binding. Although G-quadruplexes are favored in the presence of monovalent cations, there is no evidence of the latter in the thrombin complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8102368}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8102368 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8102368}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Protein/dna]]
[[Category: Protein/dna]]
[[Category: Thrombin]]
[[Category: Thrombin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:15:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:45:11 2008''

Revision as of 05:45, 1 July 2008

Image:1hut.png

Template:STRUCTURE 1hut

THE STRUCTURE OF ALPHA-THROMBIN INHIBITED BY A 15-MER SINGLE-STRANDED DNA APTAMER

Template:ABSTRACT PUBMED 8102368

About this Structure

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

Reference

The structure of alpha-thrombin inhibited by a 15-mer single-stranded DNA aptamer., Padmanabhan K, Padmanabhan KP, Ferrara JD, Sadler JE, Tulinsky A, J Biol Chem. 1993 Aug 25;268(24):17651-4. PMID:8102368

Page seeded by OCA on Tue Jul 1 08:45:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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