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| - | [[Image:2h8b.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2h8b| PDB=2h8b | SCENE= }} | | {{STRUCTURE_2h8b| PDB=2h8b | SCENE= }} |
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| - | '''Solution structure of INSL3'''
| + | ===Solution structure of INSL3=== |
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| - | ==Overview==
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| - | Insulin-like peptide 3 (INSL3), a member of the relaxin peptide family, is produced in testicular Leydig cells and ovarian thecal cells. Gene knock-out experiments have identified a key biological role in initiating testes descent during fetal development. Additionally, INSL3 has an important function in mediating male and female germ cell function. These actions are elicited via its recently identified receptor, LGR8, a member of the leucine-rich repeat-containing G-protein-coupled receptor family. To identify the structural features that are responsible for the interaction of INSL3 with its receptor, its solution structure was determined by NMR spectroscopy together with in vitro assays of a series of B-chain alanine-substituted analogs. Synthetic human INSL3 was found to adopt a characteristic relaxin/insulin-like fold in solution but is a highly dynamic molecule. The four termini of this two-chain peptide are disordered, and additional conformational exchange is evident in the molecular core. Alanine-substituted analogs were used to identify the key residues of INSL3 that are responsible for the interaction with the ectodomain of LGR8. These include Arg(B16) and Val(B19), with His(B12) and Arg(B20) playing a secondary role, as evident from the synergistic effect on the activity in double and triple mutants involving these residues. Together, these amino acids combine with the previously identified critical residue, Trp(B27), to form the receptor binding surface. The current results provide clear direction for the design of novel specific agonists and antagonists of this receptor.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16867980}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16867980 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16867980}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2H8B is a [[Protein complex]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8B OCA]. | + | 2H8B is a [[Protein complex]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H8B OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Rosengren, K J.]] | | [[Category: Rosengren, K J.]] |
| | [[Category: Insulin/relaxin suparfamily fold]] | | [[Category: Insulin/relaxin suparfamily fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:59:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:48:23 2008'' |
Revision as of 10:48, 27 July 2008
Template:STRUCTURE 2h8b
Solution structure of INSL3
Template:ABSTRACT PUBMED 16867980
About this Structure
2H8B is a Protein complex structure. Full experimental information is available from OCA.
Reference
Solution structure and characterization of the LGR8 receptor binding surface of insulin-like peptide 3., Rosengren KJ, Zhang S, Lin F, Daly NL, Scott DJ, Hughes RA, Bathgate RA, Craik DJ, Wade JD, J Biol Chem. 2006 Sep 22;281(38):28287-95. Epub 2006 Jul 25. PMID:16867980
Page seeded by OCA on Sun Jul 27 13:48:23 2008
