1jpy: Difference between revisions

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New page: left|200px<br /> <applet load="1jpy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jpy, resolution 2.85Å" /> '''Crystal structure o...
 
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[[Image:1jpy.gif|left|200px]]<br />
[[Image:1jpy.gif|left|200px]]<br /><applet load="1jpy" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1jpy" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1jpy, resolution 2.85&Aring;" />
caption="1jpy, resolution 2.85&Aring;" />
'''Crystal structure of IL-17F'''<br />
'''Crystal structure of IL-17F'''<br />


==Overview==
==Overview==
The proinflammatory cytokine interleukin 17 (IL-17) is the founding member, of a family of secreted proteins that elicit potent cellular responses. We, report a novel human IL-17 homolog, IL-17F, and show that it is expressed, by activated T cells, can stimulate production of other cytokines such as, IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate, cartilage matrix turnover. Unexpectedly, the crystal structure of IL-17F, reveals that IL-17 family members adopt a monomer fold typical of cystine, knot growth factors, despite lacking the disulfide responsible for, defining the canonical "knot" structure. IL-17F dimerizes in a parallel, manner like neurotrophins, and features an unusually large cavity on its, surface. Remarkably, this cavity is located in precisely the same position, where nerve growth factor binds its high affinity receptor, TrkA, suggesting further parallels between IL-17s and neurotrophins with respect, to receptor recognition.
The proinflammatory cytokine interleukin 17 (IL-17) is the founding member of a family of secreted proteins that elicit potent cellular responses. We report a novel human IL-17 homolog, IL-17F, and show that it is expressed by activated T cells, can stimulate production of other cytokines such as IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate cartilage matrix turnover. Unexpectedly, the crystal structure of IL-17F reveals that IL-17 family members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfide responsible for defining the canonical "knot" structure. IL-17F dimerizes in a parallel manner like neurotrophins, and features an unusually large cavity on its surface. Remarkably, this cavity is located in precisely the same position where nerve growth factor binds its high affinity receptor, TrkA, suggesting further parallels between IL-17s and neurotrophins with respect to receptor recognition.


==About this Structure==
==About this Structure==
1JPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NDG, NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JPY OCA].  
1JPY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPY OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cai, L.]]
[[Category: Cai, L.]]
[[Category: Filvaroff, E.H.]]
[[Category: Filvaroff, E H.]]
[[Category: Foster, J.]]
[[Category: Foster, J.]]
[[Category: Gurney, A.L.]]
[[Category: Gurney, A L.]]
[[Category: Hymowitz, S.G.]]
[[Category: Hymowitz, S G.]]
[[Category: Kelley, R.]]
[[Category: Kelley, R.]]
[[Category: Lee, J.]]
[[Category: Lee, J.]]
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[[Category: Pan, G.]]
[[Category: Pan, G.]]
[[Category: Risser, P.]]
[[Category: Risser, P.]]
[[Category: Starovasnik, M.A.]]
[[Category: Starovasnik, M A.]]
[[Category: Vos, A.M.de.]]
[[Category: Vos, A M.de.]]
[[Category: Yin, J.]]
[[Category: Yin, J.]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: t-cell derived]]
[[Category: t-cell derived]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:43:26 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:27 2008''

Revision as of 14:25, 21 February 2008

File:1jpy.gif


1jpy, resolution 2.85Å

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Crystal structure of IL-17F

OverviewOverview

The proinflammatory cytokine interleukin 17 (IL-17) is the founding member of a family of secreted proteins that elicit potent cellular responses. We report a novel human IL-17 homolog, IL-17F, and show that it is expressed by activated T cells, can stimulate production of other cytokines such as IL-6, IL-8 and granulocyte colony-stimulating factor, and can regulate cartilage matrix turnover. Unexpectedly, the crystal structure of IL-17F reveals that IL-17 family members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfide responsible for defining the canonical "knot" structure. IL-17F dimerizes in a parallel manner like neurotrophins, and features an unusually large cavity on its surface. Remarkably, this cavity is located in precisely the same position where nerve growth factor binds its high affinity receptor, TrkA, suggesting further parallels between IL-17s and neurotrophins with respect to receptor recognition.

About this StructureAbout this Structure

1JPY is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

IL-17s adopt a cystine knot fold: structure and activity of a novel cytokine, IL-17F, and implications for receptor binding., Hymowitz SG, Filvaroff EH, Yin JP, Lee J, Cai L, Risser P, Maruoka M, Mao W, Foster J, Kelley RF, Pan G, Gurney AL, de Vos AM, Starovasnik MA, EMBO J. 2001 Oct 1;20(19):5332-41. PMID:11574464

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