1kex

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{{Seed}}
 
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[[Image:1kex.png|left|200px]]
 
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==Crystal Structure of the b1 Domain of Human Neuropilin-1==
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The line below this paragraph, containing "STRUCTURE_1kex", creates the "Structure Box" on the page.
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<StructureSection load='1kex' size='340' side='right'caption='[[1kex]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kex]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KEX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kex OCA], [https://pdbe.org/1kex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kex RCSB], [https://www.ebi.ac.uk/pdbsum/1kex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kex ProSAT]</span></td></tr>
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{{STRUCTURE_1kex| PDB=1kex | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NRP1_HUMAN NRP1_HUMAN] The membrane-bound isoform 1 is a receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. It mediates the chemorepulsant activity of semaphorins. It binds to semaphorin 3A, The PLGF-2 isoform of PGF, The VEGF-165 isoform of VEGF and VEGF-B. Coexpression with KDR results in increased VEGF-165 binding to KDR as well as increased chemotaxis. It may regulate VEGF-induced angiogenesis. The soluble isoform 2 binds VEGF-165 and appears to inhibit its binding to cells. It may also induce apoptosis by sequestering VEGF-165. May bind as well various members of the semaphorin family. Its expression has an averse effect on blood vessel number and integrity.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ke/1kex_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kex ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal Structure of the b1 Domain of Human Neuropilin-1===
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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<ref>PMID:12517344</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kex" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12517344}}, adds the Publication Abstract to the page
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*[[Neuropilin|Neuropilin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12517344 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12517344}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1KEX is a 1 chain 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].
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==Reference==
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<ref group="xtra">PMID:12517344</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Kreusch, A.]]
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[[Category: Large Structures]]
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[[Category: Lee, C C.]]
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[[Category: Kreusch A]]
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[[Category: McMullan, D.]]
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[[Category: Lee CC]]
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[[Category: Ng, K.]]
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[[Category: McMullan D]]
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[[Category: Spraggon, G.]]
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[[Category: Ng K]]
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[[Category: Beta barrel]]
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[[Category: Spraggon G]]
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[[Category: Jelly-roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:44:20 2009''
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Current revision

Crystal Structure of the b1 Domain of Human Neuropilin-1

PDB ID 1kex

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