1qcl: Difference between revisions

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~~{{STRUCTURE_1qcl| PDB=1qcl | SCENE= }}~~

==PREDICTED STRUCTURE OF HUMAN MYELIN BASIC PROTEIN.==

===PREDICTED STRUCTURE OF HUMAN MYELIN BASIC PROTEIN.===

~~{{ABSTRACT_PUBMED_9020143}}~~

== Structural highlights ==

<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QCL FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qcl FirstGlance], [https://www.ebi.ac.uk/pdbsum/1qcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qcl ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

A computational model of myelin basic protein (MBP) has been constructed based on the premise of a phylogenetically conserved beta-sheet backbone and on electron microscopical three-dimensional reconstructions. Many residues subject to post-translational modification (phosphorylation, methylation, or conversion of arginines to citrullines) were located in loop regions and thus accessible to modifying enzymes. The triproline segment (residues 99-101) is fully exposed on the back surface of the protein in a long crossover connection between two parallel beta-strands. The proximity of this region to the underlying beta-sheet suggests that post-translational modifications here might have potential synergistic effects on the entire structure. Post-translational modifications that lead to a reduced surface charge could result first in a weakened attachment to the myelin membrane rather than in a gross conformational change of the protein itself. Such mechanisms could be operative in demyelinating diseases such as multiple sclerosis.

~~==Reference==~~

Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis.,Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G J Biol Chem. 1997 Feb 14;272(7):4269-75. PMID:9020143<ref>PMID:9020143</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Theoretical Model]]

[[Category: Large Structures]]

[[Category: Beniac, D R]]

[[Category: Harauz, G]]

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@@ Line 1: / Line 1: @@
 {{Theoretical_model}}
-{{STRUCTURE_1qcl|  PDB=1qcl  |  SCENE=  }}
+==PREDICTED STRUCTURE OF HUMAN MYELIN BASIC PROTEIN.==
-===PREDICTED STRUCTURE OF HUMAN MYELIN BASIC PROTEIN.===
+<StructureSection load='1qcl' size='340' side='right'caption='[[1qcl]]' scene=''>
-{{ABSTRACT_PUBMED_9020143}}
+== Structural highlights ==
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QCL FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qcl FirstGlance], [https://www.ebi.ac.uk/pdbsum/1qcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qcl ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A computational model of myelin basic protein (MBP) has been constructed based on the premise of a phylogenetically conserved beta-sheet backbone and on electron microscopical three-dimensional reconstructions. Many residues subject to post-translational modification (phosphorylation, methylation, or conversion of arginines to citrullines) were located in loop regions and thus accessible to modifying enzymes. The triproline segment (residues 99-101) is fully exposed on the back surface of the protein in a long crossover connection between two parallel beta-strands. The proximity of this region to the underlying beta-sheet suggests that post-translational modifications here might have potential synergistic effects on the entire structure. Post-translational modifications that lead to a reduced surface charge could result first in a weakened attachment to the myelin membrane rather than in a gross conformational change of the protein itself. Such mechanisms could be operative in demyelinating diseases such as multiple sclerosis.
-==Reference==
+Three-dimensional structure of myelin basic protein. II. Molecular modeling and considerations of predicted structures in multiple sclerosis.,Ridsdale RA, Beniac DR, Tompkins TA, Moscarello MA, Harauz G J Biol Chem. 1997 Feb 14;272(7):4269-75. PMID:9020143<ref>PMID:9020143</ref>
-<ref group="xtra">PMID:009020143</ref><references group="xtra"/><references/>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qcl" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Theoretical Model]]
+[[Category: Large Structures]]
 [[Category: Beniac, D R]]
 [[Category: Harauz, G]]