1neu: Difference between revisions

Revision as of 23:19, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1neu.png

Template:STRUCTURE 1neu

STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0

Template:ABSTRACT PUBMED 8816707

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

Page seeded by OCA on Sun Jul 27 23:19:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1neu.gif|left|200px]]
+{{Seed}}
+[[Image:1neu.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1neu|  PDB=1neu  |  SCENE=  }}
-'''STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0'''
+===STRUCTURE OF MYELIN MEMBRANE ADHESION MOLECULE P0===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8816707}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8816707 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8816707}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Structural protein]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:26:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:19:35 2008''