1imv

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(New page: 200px<br /> <applet load="1imv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imv, resolution 2.85&Aring;" /> '''2.85 A crystal stru...)
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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==
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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.
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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==
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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].
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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==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Gettins, P.G.W.]]
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[[Category: Gettins, P G.W.]]
[[Category: Simonovic, M.]]
[[Category: Simonovic, M.]]
[[Category: Volz, K.]]
[[Category: Volz, K.]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:31:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:28 2008''

Revision as of 11:13, 21 February 2008

Image:1imv.gif

1imv, resolution 2.85Å

Drag the structure with the mouse to rotate

2.85 A crystal structure of PEDF

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.

About this Structure

1IMV is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor., Simonovic M, Gettins PG, Volz K, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11131-5. Epub 2001 Sep 18. PMID:11562499

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