1kex: Difference between revisions

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[[Image:1kex.gif|left|200px]]<br />

[[Image:1kex.gif|left|200px]]<br /><applet load="1kex" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1kex" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1kex, resolution 1.9Å" />

'''Crystal Structure of the b1 Domain of Human Neuropilin-1'''<br />

==Overview==

Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad, range of developmental processes, including axon guidance, angiogenesis, and heterophilic cell adhesion. We have determined the crystal structure, of the human Npn-1 b1 domain to 1.9 A. The overall structure resembles, coagulation factor V and VIII (F5/8) C1 and C2 domains, exhibiting a, distorted jellyroll fold. Details of the structure provide insight to b1, domain regions responsible for ligand binding and facilitate, rationalization of existing biochemical binding data. A polar cleft formed, by adjacent loops at one end of the molecule in conjunction with flanking, electronegative surfaces may represent the binding site for the positively, charged tails of semaphorins and VEGF(165). The nature of the cell, adhesion binding site of the b1 domain can be visualized in context of the, structure.

Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad range of developmental processes, including axon guidance, angiogenesis, and heterophilic cell adhesion. We have determined the crystal structure of the human Npn-1 b1 domain to 1.9 A. The overall structure resembles coagulation factor V and VIII (F5/8) C1 and C2 domains, exhibiting a distorted jellyroll fold. Details of the structure provide insight to b1 domain regions responsible for ligand binding and facilitate rationalization of existing biochemical binding data. A polar cleft formed by adjacent loops at one end of the molecule in conjunction with flanking electronegative surfaces may represent the binding site for the positively charged tails of semaphorins and VEGF(165). The nature of the cell adhesion binding site of the b1 domain can be visualized in context of the structure.

==Disease==

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==About this Structure==

1KEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1KEX OCA].

1KEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEX OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Kreusch, A.]]

[[Category: Lee, C.C.]]

[[Category: Lee, C C.]]

[[Category: McMullan, D.]]

[[Category: Ng, K.]]

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[[Category: jelly-roll]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 17~~:50:~~29 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1kex.gif|left|200px]]<br />
+[[Image:1kex.gif|left|200px]]<br /><applet load="1kex" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1kex" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1kex, resolution 1.9&Aring;" />
 '''Crystal Structure of the b1 Domain of Human Neuropilin-1'''<br />
 ==Overview==
-Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad, range of developmental processes, including axon guidance, angiogenesis, and heterophilic cell adhesion. We have determined the crystal structure, of the human Npn-1 b1 domain to 1.9 A. The overall structure resembles, coagulation factor V and VIII (F5/8) C1 and C2 domains, exhibiting a, distorted jellyroll fold. Details of the structure provide insight to b1, domain regions responsible for ligand binding and facilitate, rationalization of existing biochemical binding data. A polar cleft formed, by adjacent loops at one end of the molecule in conjunction with flanking, electronegative surfaces may represent the binding site for the positively, charged tails of semaphorins and VEGF(165). The nature of the cell, adhesion binding site of the b1 domain can be visualized in context of the, structure.
+Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad range of developmental processes, including axon guidance, angiogenesis, and heterophilic cell adhesion. We have determined the crystal structure of the human Npn-1 b1 domain to 1.9 A. The overall structure resembles coagulation factor V and VIII (F5/8) C1 and C2 domains, exhibiting a distorted jellyroll fold. Details of the structure provide insight to b1 domain regions responsible for ligand binding and facilitate rationalization of existing biochemical binding data. A polar cleft formed by adjacent loops at one end of the molecule in conjunction with flanking electronegative surfaces may represent the binding site for the positively charged tails of semaphorins and VEGF(165). The nature of the cell adhesion binding site of the b1 domain can be visualized in context of the structure.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-KEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KEX OCA].
+KEX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEX OCA].
 ==Reference==
@@ Line 18: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Kreusch, A.]]
-[[Category: Lee, C.C.]]
+[[Category: Lee, C C.]]
 [[Category: McMullan, D.]]
 [[Category: Ng, K.]]
@@ Line 25: / Line 24: @@
 [[Category: jelly-roll]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:50:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:21 2008''