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2fhw
From Proteopedia
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| - | [[Image:2fhw.gif|left|200px]] | + | [[Image:2fhw.gif|left|200px]] |
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| - | '''Solution structure of human relaxin-3''' | + | {{Structure |
| + | |PDB= 2fhw |SIZE=350|CAPTION= <scene name='initialview01'>2fhw</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of human relaxin-3''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FHW is a [ | + | 2FHW is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FHW OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16365033 16365033] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Craik, D J.]] | [[Category: Craik, D J.]] | ||
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[[Category: insulin/relaxin super-family fold]] | [[Category: insulin/relaxin super-family fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:52:37 2008'' |
Revision as of 14:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 of sequences from [1]. 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 Thu Mar 20 16:52:37 2008
