2fbe: Difference between revisions

Line 1:

[[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"

<applet load="2fbe" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2fbe, resolution 2.52Å" />

'''Crystal Structure of the PRYSPRY-domain'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FBE OCA].

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==

Line 17:

Line 16:

[[Category: Capitani, G.]]

[[Category: Gruetter, C.]]

[[Category: Gruetter, M.G.]]

[[Category: Gruetter, M G.]]

[[Category: Mittl, P.R.]]

[[Category: Mittl, P R.]]

[[Category: dimer]]

[[Category: jellyroll beta-sandwich fold]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:02:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:38 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[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"
-<applet load="2fbe" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2fbe, resolution 2.52&Aring;" />
 '''Crystal Structure of the PRYSPRY-domain'''<br />
 ==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.
+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==
-FBE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FBE OCA].
+FBE 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==
@@ Line 17: / Line 16: @@
 [[Category: Capitani, G.]]
 [[Category: Gruetter, C.]]
-[[Category: Gruetter, M.G.]]
+[[Category: Gruetter, M G.]]
-[[Category: Mittl, P.R.]]
+[[Category: Mittl, P R.]]
 [[Category: dimer]]
 [[Category: jellyroll beta-sandwich fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:02:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:38 2008''