2fhw
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2fhw.gif|left|200px]] | [[Image:2fhw.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2fhw", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_2fhw| PDB=2fhw | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Solution structure of human relaxin-3''' | '''Solution structure of human relaxin-3''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2FHW is a [[Protein complex]] structure | + | 2FHW is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHW OCA]. |
==Reference== | ==Reference== | ||
| Line 26: | Line 23: | ||
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
[[Category: Rosengren, K J.]] | [[Category: Rosengren, K J.]] | ||
| - | [[Category: | + | [[Category: Insulin/relaxin super-family fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:55:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:55, 4 May 2008
Solution structure of human relaxin-3
Overview
Relaxin-3 is the most recently discovered member of the relaxin family of peptide hormones. In contrast to relaxin-1 and -2, whose main functions are associated with pregnancy, relaxin-3 is involved in neuropeptide signaling in the brain. Here, we report the solution structure of human relaxin-3, the first structure of a relaxin family member to be solved by NMR methods. Overall, relaxin-3 adopts an insulin-like fold, but the structure differs crucially from the crystal structure of human relaxin-2 near the B-chain terminus. In particular, the B-chain C terminus folds back, allowing Trp(B27) to interact with the hydrophobic core. This interaction partly blocks the conserved RXXXRXXI motif identified as a determinant for the interaction with the relaxin receptor LGR7 and may account for the lower affinity of relaxin-3 relative to relaxin for this receptor. This structural feature is likely important for the activation of its endogenous receptor, GPCR135.
About this Structure
2FHW is a Protein complex structure. Full crystallographic information is available from OCA.
Reference
Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3., Rosengren KJ, Lin F, Bathgate RA, Tregear GW, Daly NL, Wade JD, Craik DJ, J Biol Chem. 2006 Mar 3;281(9):5845-51. Epub 2005 Dec 19. PMID:16365033 Page seeded by OCA on Sun May 4 03:55:07 2008
