1kn3

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(New page: 200px<br /><applet load="1kn3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kn3, resolution 1.80&Aring;" /> '''Murine PEBP-2 (phosp...)
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[[Image:1kn3.gif|left|200px]]<br /><applet load="1kn3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kn3, resolution 1.80&Aring;" />
caption="1kn3, resolution 1.80&Aring;" />
'''Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)'''<br />
'''Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)'''<br />
==Overview==
==Overview==
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Proteins from the PEBP (phosphatidylethanolamine-binding protein) family, have been identified in a wide variety of species and are thought to, regulate a range of intracellular signalling cascades. The rat homologue, (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to, negatively regulate the MAP kinase pathway through formation of inhibitory, complexes with Raf-1 and MEK. The crystal structure of a new, murine, member of the PEBP family, termed mPEBP-2, has been determined. On the, basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the, mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar, in structure to other PEBP proteins from human, bovine and plant sources., Regions of distinctive sequence associated with the PEBP-2 subset are, discussed with reference to this structure.
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Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have been identified in a wide variety of species and are thought to regulate a range of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to negatively regulate the MAP kinase pathway through formation of inhibitory complexes with Raf-1 and MEK. The crystal structure of a new, murine member of the PEBP family, termed mPEBP-2, has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar in structure to other PEBP proteins from human, bovine and plant sources. Regions of distinctive sequence associated with the PEBP-2 subset are discussed with reference to this structure.
==About this Structure==
==About this Structure==
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1KN3 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KN3 OCA].
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1KN3 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=1KN3 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Banfield, M.J.]]
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[[Category: Banfield, M J.]]
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[[Category: Brady, R.L.]]
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[[Category: Brady, R L.]]
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[[Category: Simister, P.C.]]
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[[Category: Simister, P C.]]
[[Category: cis-peptide]]
[[Category: cis-peptide]]
[[Category: phosphatidylethanolamine binding]]
[[Category: phosphatidylethanolamine binding]]
[[Category: raf-1 kinase inhibitor]]
[[Category: raf-1 kinase inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:22:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:54 2008''

Revision as of 11:35, 21 February 2008

Image:1kn3.gif

1kn3, resolution 1.80Å

Drag the structure with the mouse to rotate

Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)

Overview

Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have been identified in a wide variety of species and are thought to regulate a range of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to negatively regulate the MAP kinase pathway through formation of inhibitory complexes with Raf-1 and MEK. The crystal structure of a new, murine member of the PEBP family, termed mPEBP-2, has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar in structure to other PEBP proteins from human, bovine and plant sources. Regions of distinctive sequence associated with the PEBP-2 subset are discussed with reference to this structure.

About this Structure

1KN3 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family., Simister PC, Banfield MJ, Brady RL, Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1077-80. Epub, 2002 May 29. PMID:12037323

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