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.


1wso

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wso.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wso.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wso| PDB=1wso | SCENE= }}
{{STRUCTURE_1wso| PDB=1wso | SCENE= }}
-
'''The solution structures of human Orexin-A'''
+
===The solution structures of human Orexin-A===
-
==Overview==
+
<!--
-
Orexins-A and B, also called hypocretins-1 and 2, respectively, are neuropeptides that regulate feeding and sleep-wakefulness by binding to two orphan G protein-coupled receptors named orexin-1 (OX(1)R) and orexin-2 (OX(2)R). The sequences and functions of orexins-A and B are similar to each other, but the high sequence homology (68%) is limited in their C-terminal half regions (residues 15-33). The sequence of the N-terminal half region of orexin-A (residues 1-14), containing two disulfide bonds, is very different from that of orexin-B. The structure of orexin-A was determined using two-dimensional homonuclear and (15)N and (13)C natural abundance heteronuclear NMR experiments. Orexin-A had a compact conformation in the N-terminal half region, which contained a short helix (III:Cys6-Gln9) and was fixed by the two disulfide bonds, and a helix-turn-helix conformation (I:Leu16-Ala23 and II:Asn25-Thr32) in the remaining C-terminal half region. The C-terminal half region had both hydrophobic and hydrophilic residues, which existed on separate surfaces to provide an amphipathic character in helices I and II. The nine residues on the hydrophobic surface are also well conserved in orexin-B, and it was reported that the substitution of each of them with alanine resulted in a significant drop in the functional potency at the receptors. Therefore, we suggest that they form the surface responsible for the main hydrophobic interaction with the receptors. On the other hand, the residues on the hydrophilic surface, together with the hydrophilic residues in the N-terminal half region that form a cluster, are known to make only small contributions to the binding to the receptors through similar alanine-scan experiments. However, since our structure of orexin-A showed that large conformational and electrostatical differences between orexins-A and B were rather concentrated in the N-terminal half regions, we suggest that the region of orexin-A is important for the preference for orexin-A of OX(1)R.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16429482}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16429482 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16429482}}
==About this Structure==
==About this Structure==
-
1WSO is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSO OCA].
+
1WSO is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSO OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Orexin]]
[[Category: Orexin]]
[[Category: Orphan g-protein coupled receptor]]
[[Category: Orphan g-protein coupled receptor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:27:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:00:23 2008''

Revision as of 06:00, 28 July 2008

Image:1wso.png

Template:STRUCTURE 1wso

The solution structures of human Orexin-A

Template:ABSTRACT PUBMED 16429482

About this Structure

1WSO is a Single protein structure. Full experimental information is available from OCA.

Reference

Orexin-A is composed of a highly conserved C-terminal and a specific, hydrophilic N-terminal region, revealing the structural basis of specific recognition by the orexin-1 receptor., Takai T, Takaya T, Nakano M, Akutsu H, Nakagawa A, Aimoto S, Nagai K, Ikegami T, J Pept Sci. 2006 Jul;12(7):443-54. PMID:16429482

Page seeded by OCA on Mon Jul 28 09:00:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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