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.


1hic

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hic.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hic.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hic| PDB=1hic | SCENE= }}
{{STRUCTURE_1hic| PDB=1hic | SCENE= }}
-
'''THE NMR SOLUTION STRUCTURE OF HIRUDIN(1-51) AND COMPARISON WITH CORRESPONDING THREE-DIMENSIONAL STRUCTURES DETERMINED USING THE COMPLETE 65-RESIDUE HIRUDIN POLYPEPTIDE CHAIN'''
+
===THE NMR SOLUTION STRUCTURE OF HIRUDIN(1-51) AND COMPARISON WITH CORRESPONDING THREE-DIMENSIONAL STRUCTURES DETERMINED USING THE COMPLETE 65-RESIDUE HIRUDIN POLYPEPTIDE CHAIN===
-
==Overview==
+
<!--
-
The three-dimensional structure of the N-terminal 51-residue domain of recombinant hirudin in aqueous solution was determined by 1H nuclear magnetic resonance (NMR) spectroscopy, and the resulting high-quality solution structure was compared with corresponding structures obtained from studies with the intact, 65-residue polypeptide chain of hirudin. On the basis of 580 distance constraints derived from nuclear Overhauser effects and 109 dihedral angle constraints, a group of 20 conformers representing the solution structure of hirudin(1-51) was computed with the program DIANA and energy-minimized with a modified version of the program AMBER. Residues 3 to 30 and 37 to 48 form a well-defined molecular core with two antiparallel beta-sheets composed of residues 14 to 16 and 20 to 22, and 27 to 31 and 36 to 40, and three reverse turns at residues 8 to 11 (type II), 17 to 20 (type II') and 23 to 26 (type II). The average root-mean-square deviation of the individual NMR conformers relative to their mean co-ordinates is 0.38 A for the backbone atoms and 0.77 A for all heavy atoms of these residues. Increased structural disorder was found for the N-terminal dipeptide segment, the loop at residues 31 to 36, and the C-terminal tripeptide segment. The solution structure of hirudin(1-51) has the same molecular architecture as the corresponding polypeptide segment in natural hirudin and recombinant desulfatohirudin. It is also closely similar to the crystal structure of the N-terminal 51-residue segment of hirudin in a hirudin-thrombin complex, with root-mean-square deviations of the crystal structure relative to the mean solution structure of 0.61 A for the backbone atoms and 0.91 A for all heavy atoms of residues 3 to 30 and 37 to 48. Further coincidence is found for the loop formed by residues 31 to 36, which shows increased structural disorder in all available solution structures of hirudin, and of which residues 32 to 35 are not observable in the electron density map of the thrombin complex. Significant local structural differences between hirudin(1-51) in solution and hirudin in the crystalline thrombin complex were identified mainly for the N-terminal tripeptide segment and residues 17 to 21. These are further analyzed in an accompanying paper.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1335515}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1335515 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1335515}}
==About this Structure==
==About this Structure==
-
1HIC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIC OCA].
+
1HIC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIC OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
[[Category: Hirudin]]
[[Category: Hirudin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:52:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:13:32 2008''

Revision as of 05:13, 1 July 2008

Image:1hic.png

Template:STRUCTURE 1hic

THE NMR SOLUTION STRUCTURE OF HIRUDIN(1-51) AND COMPARISON WITH CORRESPONDING THREE-DIMENSIONAL STRUCTURES DETERMINED USING THE COMPLETE 65-RESIDUE HIRUDIN POLYPEPTIDE CHAIN

Template:ABSTRACT PUBMED 1335515

About this Structure

1HIC is a Single protein structure of sequence from Hirudo medicinalis. Full experimental information is available from OCA.

Reference

Nuclear magnetic resonance solution structure of hirudin(1-51) and comparison with corresponding three-dimensional structures determined using the complete 65-residue hirudin polypeptide chain., Szyperski T, Guntert P, Stone SR, Wuthrich K, J Mol Biol. 1992 Dec 20;228(4):1193-205. PMID:1335515

Page seeded by OCA on Tue Jul 1 08:13:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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