1rgx
From Proteopedia
(New page: 200px<br /><applet load="1rgx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rgx, resolution 1.787Å" /> '''Crystal Structure o...) |
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| - | [[Image:1rgx.gif|left|200px]]<br /><applet load="1rgx" size=" | + | [[Image:1rgx.gif|left|200px]]<br /><applet load="1rgx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rgx, resolution 1.787Å" /> | caption="1rgx, resolution 1.787Å" /> | ||
'''Crystal Structure of resisitin'''<br /> | '''Crystal Structure of resisitin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Resistin, founding member of the resistin-like molecule (RELM) hormone | + | Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation. |
==About this Structure== | ==About this Structure== | ||
| - | 1RGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1RGX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: NYSGXRC, New | + | [[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]] |
| - | [[Category: Patel, S | + | [[Category: Patel, S D.]] |
| - | [[Category: Rajala, M | + | [[Category: Rajala, M W.]] |
| - | [[Category: Scherer, P | + | [[Category: Scherer, P E.]] |
[[Category: Shapiro, L.]] | [[Category: Shapiro, L.]] | ||
[[Category: hormone; glucose uptake; resistin/fizz family]] | [[Category: hormone; glucose uptake; resistin/fizz family]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:45 2008'' |
Revision as of 12:50, 21 February 2008
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Crystal Structure of resisitin
Overview
Resistin, founding member of the resistin-like molecule (RELM) hormone family, is secreted selectively from adipocytes and induces liver-specific antagonism of insulin action, thus providing a potential molecular link between obesity and diabetes. Crystal structures of resistin and RELMbeta reveal an unusual multimeric structure. Each protomer comprises a carboxy-terminal disulfide-rich beta-sandwich "head" domain and an amino-terminal alpha-helical "tail" segment. The alpha-helical segments associate to form three-stranded coiled coils, and surface-exposed interchain disulfide linkages mediate the formation of tail-to-tail hexamers. Analysis of serum samples shows that resistin circulates in two distinct assembly states, likely corresponding to hexamers and trimers. Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin. This result suggests that processing of the intertrimer disulfide bonds may reflect an obligatory step toward activation.
About this Structure
1RGX is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Disulfide-dependent multimeric assembly of resistin family hormones., Patel SD, Rajala MW, Rossetti L, Scherer PE, Shapiro L, Science. 2004 May 21;304(5674):1154-8. PMID:15155948
Page seeded by OCA on Thu Feb 21 14:50:45 2008
Categories: Mus musculus | Single protein | Burley, S K. | NYSGXRC, New York Structural GenomiX Research Consortium. | Patel, S D. | Rajala, M W. | Scherer, P E. | Shapiro, L. | Hormone; glucose uptake; resistin/fizz family | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomics
