1neu: Difference between revisions
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[[Image:1neu.gif|left|200px]] | [[Image:1neu.gif|left|200px]] | ||
'''STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0''' | {{Structure | ||
|PDB= 1neu |SIZE=350|CAPTION= <scene name='initialview01'>1neu</scene>, resolution 1.9Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
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'''STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NEU is a [ | 1NEU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NEU OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin., Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA, Neuron. 1996 Sep;17(3):435-49. PMID:[http:// | Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin., Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA, Neuron. 1996 Sep;17(3):435-49. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8816707 8816707] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:58 2008'' | ||
Revision as of 13:55, 20 March 2008
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STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0
OverviewOverview
P0, the major protein of peripheral nerve myelin, mediates membrane adhesion in the spiral wraps of the myelin sheath. We have determined the crystal structure of the extracellular domain from P0 (P0ex) at 1.9 A resolution. P0ex is folded like a typical immunoglobulin variable-like domain; five residues at the C-terminus are disordered, suggesting a flexible linkage to the membrane. The requirements for crystallization of P0ex are similar to those for maintaining the native extracellular spacing of adjacent myelin lamellae; thus, given the self-adhesive character of P0ex, the crystal itself may reveal some of the natural interactions that occur between P0 molecules in myelin. The structure leads to the suggestion that P0 extracellular domains may emanate from the membrane surface as tetramers that link to tetramers on the opposing membrane surface, to result in the formation of networks of molecules. We report analytical ultracentrifugation data for P0ex that support this idea.
About this StructureAbout this Structure
1NEU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the extracellular domain from P0, the major structural protein of peripheral nerve myelin., Shapiro L, Doyle JP, Hensley P, Colman DR, Hendrickson WA, Neuron. 1996 Sep;17(3):435-49. PMID:8816707
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