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.


1hlt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hlt.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hlt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hlt| PDB=1hlt | SCENE= }}
{{STRUCTURE_1hlt| PDB=1hlt | SCENE= }}
-
'''THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN'''
+
===THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN===
-
==Overview==
+
<!--
-
The crystallographic structure has been determined of a complex between a nonadecapeptide from the fifth epidermal growth factor (EGF5) domain of human thrombomodulin and human D-PheProArg-alpha-thrombin. The peptide corresponds to amino acid residues Glu408-Glu426 of thrombomodulin and contains the third disulfide loop of EGF5 and its linker to EGF6. The structure was refined at 3.0-A resolution to an R-value of 0.146. There are two thrombin molecules in the asymmetric unit, and the structure in the crystal is a 2:1 thrombin complex. The folding of the peptide corresponds closely to the third disulfide loop of EGF2 of factor Xa (rms delta = 1.0 A). The peptide is squeezed between cofacial electropositive fibrinogen recognition exo sites of the two thrombin molecules. Since the peptide has a total of seven aspartic and glutamic acid residues, the principal binding interaction with thrombin is electrostatic. A major hydrophobic association, which is highly directional in such a pronounced electrostatic environment, involves a TyrIleLeu triplet of the peptide and Phe34, Leu65, Tyr76, and Ile82 (chymotrypsinogen numbering) of one thrombin molecule. The tyrosine of the peptide is sandwiched between the thrombin aromatic rings and is most likely the prime source of the specificity of the thrombomodulin-thrombin interaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7947765}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7947765 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7947765}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Mathews, I I.]]
[[Category: Mathews, I I.]]
[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:59:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:22:20 2008''

Revision as of 05:22, 1 July 2008

Image:1hlt.png

Template:STRUCTURE 1hlt

THE STRUCTURE OF A NONADECAPEPTIDE OF THE FIFTH EGF DOMAIN OF THROMBOMODULIN COMPLEXED WITH THROMBIN

Template:ABSTRACT PUBMED 7947765

About this Structure

1HLT is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin., Mathews II, Padmanabhan KP, Tulinksy A, Sadler JE, Biochemistry. 1994 Nov 22;33(46):13547-52. PMID:7947765

Page seeded by OCA on Tue Jul 1 08:22:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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