2fbe: Difference between revisions
New page: left|200px<br /> <applet load="2fbe" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fbe, resolution 2.52Å" /> '''Crystal Structure o... |
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[[Image:2fbe.gif|left|200px]]<br /> | [[Image:2fbe.gif|left|200px]]<br /><applet load="2fbe" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Crystal Structure of the PRYSPRY-domain'''<br /> | '''Crystal Structure of the PRYSPRY-domain'''<br /> | ||
==Overview== | ==Overview== | ||
We determined the first structure of PRYSPRY, a domain found in over 500 | We determined the first structure of PRYSPRY, a domain found in over 500 different proteins, involved in innate immune signaling, cytokine signaling suppression, development, cell growth and retroviral restriction. The fold encompasses a 7-stranded and a 6-stranded antiparallel beta-sheet, arranged in a beta-sandwich. In the crystal, PRYSPRY forms a dimer where the C-terminus of an acceptor molecule binds to the concave surface of a donor molecule, which represents a putative interaction site. Mutations in the PRYSPRY domains of Pyrin, which are responsible for familial Mediterranean fever, map on the putative PRYSPRY interaction site. | ||
==About this Structure== | ==About this Structure== | ||
2FBE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2FBE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FBE OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Capitani, G.]] | [[Category: Capitani, G.]] | ||
[[Category: Gruetter, C.]] | [[Category: Gruetter, C.]] | ||
[[Category: Gruetter, M | [[Category: Gruetter, M G.]] | ||
[[Category: Mittl, P | [[Category: Mittl, P R.]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
[[Category: jellyroll beta-sandwich fold]] | [[Category: jellyroll beta-sandwich fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:38 2008'' | ||
Revision as of 15:19, 21 February 2008
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Crystal Structure of the PRYSPRY-domain
Overview
We determined the first structure of PRYSPRY, a domain found in over 500 different proteins, involved in innate immune signaling, cytokine signaling suppression, development, cell growth and retroviral restriction. The fold encompasses a 7-stranded and a 6-stranded antiparallel beta-sheet, arranged in a beta-sandwich. In the crystal, PRYSPRY forms a dimer where the C-terminus of an acceptor molecule binds to the concave surface of a donor molecule, which represents a putative interaction site. Mutations in the PRYSPRY domains of Pyrin, which are responsible for familial Mediterranean fever, map on the putative PRYSPRY interaction site.
About this Structure
2FBE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the PRYSPRY-domain: implications for autoinflammatory diseases., Grutter C, Briand C, Capitani G, Mittl PR, Papin S, Tschopp J, Grutter MG, FEBS Lett. 2006 Jan 9;580(1):99-106. Epub 2005 Dec 9. PMID:16364311
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