1kex
From Proteopedia
(New page: 200px<br /> <applet load="1kex" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kex, resolution 1.9Å" /> '''Crystal Structure of...) |
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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" |
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caption="1kex, resolution 1.9Å" /> | caption="1kex, resolution 1.9Å" /> | ||
'''Crystal Structure of the b1 Domain of Human Neuropilin-1'''<br /> | '''Crystal Structure of the b1 Domain of Human Neuropilin-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Neuropilin-1 (Npn-1) is a type I cell surface receptor involved in a broad | + | 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== | ==Disease== | ||
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==About this Structure== | ==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:// | + | 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== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kreusch, A.]] | [[Category: Kreusch, A.]] | ||
| - | [[Category: Lee, C | + | [[Category: Lee, C C.]] |
[[Category: McMullan, D.]] | [[Category: McMullan, D.]] | ||
[[Category: Ng, K.]] | [[Category: Ng, K.]] | ||
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[[Category: jelly-roll]] | [[Category: jelly-roll]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:21 2008'' |
Revision as of 11:33, 21 February 2008
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Crystal Structure of the b1 Domain of Human Neuropilin-1
Contents |
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.
Disease
Known diseases associated with this structure: Glaucoma 1, open angle, E OMIM:[602432], Glaucoma, normal tension, susceptibility to OMIM:[602432]
About this Structure
1KEX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human neuropilin-1 b1 domain., Lee CC, Kreusch A, McMullan D, Ng K, Spraggon G, Structure. 2003 Jan;11(1):99-108. PMID:12517344
Page seeded by OCA on Thu Feb 21 13:33:21 2008
