1imv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /> <applet load="1imv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imv, resolution 2.85Å" /> '''2.85 A crystal stru...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1imv.gif|left|200px]]<br />
[[Image:1imv.gif|left|200px]]<br /><applet load="1imv" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1imv" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1imv, resolution 2.85&Aring;" />
caption="1imv, resolution 2.85&Aring;" />
'''2.85 A crystal structure of PEDF'''<br />
'''2.85 A crystal structure of PEDF'''<br />


==Overview==
==Overview==
Pigment epithelium-derived factor (PEDF), a noninhibitory member of the, serpin superfamily, is the most potent inhibitor of angiogenesis in the, mammalian ocular compartment. It also has neurotrophic activity, both in, the retina and in the central nervous system, and is highly up-regulated, in young versus senescent fibroblasts. To provide a structural basis for, understanding its many biological roles, we have solved the crystal, structure of glycosylated human PEDF to 2.85 A. The structure revealed the, organization of possible receptor and heparin-binding sites, and showed, that, unlike any other previously characterized serpin, PEDF has a, striking asymmetric charge distribution that might be of functional, importance. These results provide a starting point for future detailed, structure/function analyses into possible mechanisms of PEDF action that, could lead to development of therapeutics against uncontrolled, angiogenesis.
Pigment epithelium-derived factor (PEDF), a noninhibitory member of the serpin superfamily, is the most potent inhibitor of angiogenesis in the mammalian ocular compartment. It also has neurotrophic activity, both in the retina and in the central nervous system, and is highly up-regulated in young versus senescent fibroblasts. To provide a structural basis for understanding its many biological roles, we have solved the crystal structure of glycosylated human PEDF to 2.85 A. The structure revealed the organization of possible receptor and heparin-binding sites, and showed that, unlike any other previously characterized serpin, PEDF has a striking asymmetric charge distribution that might be of functional importance. These results provide a starting point for future detailed structure/function analyses into possible mechanisms of PEDF action that could lead to development of therapeutics against uncontrolled angiogenesis.


==About this Structure==
==About this Structure==
1IMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IMV OCA].  
1IMV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMV OCA].  


==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Gettins, P.G.W.]]
[[Category: Gettins, P G.W.]]
[[Category: Simonovic, M.]]
[[Category: Simonovic, M.]]
[[Category: Volz, K.]]
[[Category: Volz, K.]]
Line 22: Line 21:
[[Category: serpin]]
[[Category: serpin]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:31:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:28 2008''