1kex

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==Crystal Structure of the b1 Domain of Human Neuropilin-1==
==Crystal Structure of the b1 Domain of Human Neuropilin-1==
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<StructureSection load='1kex' size='340' side='right' caption='[[1kex]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='1kex' size='340' side='right'caption='[[1kex]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1kex]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KEX FirstGlance]. <br>
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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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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nrp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kex OCA], [http://pdbe.org/1kex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kex RCSB], [http://www.ebi.ac.uk/pdbsum/1kex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kex ProSAT]</span></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>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ke/1kex_consurf.spt"</scriptWhenChecked>
<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/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</div>
</div>
<div class="pdbe-citations 1kex" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1kex" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Neuropilin|Neuropilin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[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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[[Category: Protein binding]]
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Current revision

Crystal Structure of the b1 Domain of Human Neuropilin-1

PDB ID 1kex

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