<?xml version="1.0" encoding="utf-8"?>
<rss version="2.0"
					xmlns:content="http://purl.org/rss/1.0/modules/content/"
					xmlns:wfw="http://wellformedweb.org/CommentAPI/"
				  >
<channel>
<title>BUniverse: Videos by hamel </title>
<link>https://www.bu.edu/buniverse/search/?q=&amp;sort=relevance&amp;view=thumbnail&amp;owner=hamel&amp;tag=</link>
<description><![CDATA[BUniverse: Videos by hamel ]]></description>
<item>
<title>BMB 2</title>
<link>https://www.bu.edu/buniverse/view/?v=1syO9B1F8</link>
<guid>https://www.bu.edu/buniverse/view/?v=1syO9B1F8</guid>
<pubDate>Mon, 22 Apr 2013 11:10:24 -0400</pubDate>
<description><![CDATA[Version 2]]></description>
</item>
<item>
<title>The Structural Basis of Congenital Disorder of Glycosylation Type 1a</title>
<link>https://www.bu.edu/buniverse/view/?v=Grasx1F7</link>
<guid>https://www.bu.edu/buniverse/view/?v=Grasx1F7</guid>
<pubDate>Mon, 22 Apr 2013 11:05:52 -0400</pubDate>
<description><![CDATA[The structure presented here is the human enzyme, phosphomannomutase 1, bound to its substrate, mannose 1-phosphate (M1P).  There are 2 isoforms of this enzyme in humansâ€”PMM1 and PMM2, both of which catalyzes the reaction between a mannose 1-phosphate to a mannose 6-phosphate with comparable catalytic efficiency.  A decrease in PMM2 activity results in a disease called Congenital Disorder of Glycosylation type 1a (CDG-1a) characterized by severe defects mainly involving the nervous system.  In addition to similar kinetic properties, PMM1 and PMM2 also have similar structural features and a conversed active site, therefore, this structure of PMM1 bound to substrate M1P gives us insight to the structural basis of CDG-1a causing mutations. 

This structure was solved by Nicholas R. Silvaggi]]></description>
</item>
</channel>
</rss>