1rgx: Difference between revisions
New page: left|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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
