2rmi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
|PDB= 2rmi |SIZE=350|CAPTION= <scene name='initialview01'>2rmi</scene>
|PDB= 2rmi |SIZE=350|CAPTION= <scene name='initialview01'>2rmi</scene>
|SITE=
|SITE=
-
|LIGAND=
+
|LIGAND= <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[2rm9|2rm9]], [[2rmd|2rmd]], [[2rme|2rme]], [[2rmf|2rmf]], [[2rmg|2rmg]], [[2rmh|2rmh]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rmi OCA], [http://www.ebi.ac.uk/pdbsum/2rmi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2rmi RCSB]</span>
}}
}}
Line 33: Line 36:
[[Category: urotensin]]
[[Category: urotensin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:37:31 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:02:00 2008''

Revision as of 02:02, 31 March 2008

Image:2rmi.gif


PDB ID 2rmi

Drag the structure with the mouse to rotate
Ligands: ,
Related: 2rm9, 2rmd, 2rme, 2rmf, 2rmg, 2rmh


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



3D NMR structure of astressin


Overview

The C-terminally amidated CRF antagonist astressin binds to CRF-R1 or CRF-R2 receptors with low nanomolar affinity while the corresponding astressin-acid has >100 times less affinity. To understand the role of the amide group in binding, the conformations of astressin-amide and astressin-acid were studied in DMSO using NMR techniques. The 3D NMR structures show that the backbones of both analogs prefer an alpha-helical conformation, with a small kink around Gln(26). However, astressin-amide has a well-defined helical structure from Leu(27) to Ile(41) and a conformation very similar to the bioactive conformation reported by our group (Grace et al., Proc Natl Acad Sci USA 2007, 104, 4858-4863). In contrast, astressin-acid has an irregular helical conformation from Arg(35) onward, including a rearrangement of the side chains in that region. This structural difference highlights the crucial role of the C-terminal amidation for stabilization of astressin's bioactive conformation.

About this Structure

2RMI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Astressin-amide and astressin-acid are structurally different in dimethylsulfoxide., Grace CR, Cervini L, Gulyas J, Rivier J, Riek R, Biopolymers. 2007 Oct 5-15;87(2-3):196-205. PMID:17657708

Page seeded by OCA on Mon Mar 31 05:02:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rmi"
Personal tools