3q2u

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<StructureSection load='3q2u' size='340' side='right'caption='[[3q2u]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3q2u' size='340' side='right'caption='[[3q2u]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3q2u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q2U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3q2u]] 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=3Q2U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q2U FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3q2r|3q2r]], [[1u53|1u53]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLIPR, GLIPR1, RTVP1, synthesized ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3q2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2u OCA], [https://pdbe.org/3q2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q2u RCSB], [https://www.ebi.ac.uk/pdbsum/3q2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q2u ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3q2u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2u OCA], [https://pdbe.org/3q2u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q2u RCSB], [https://www.ebi.ac.uk/pdbsum/3q2u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q2u ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/GLIP1_HUMAN GLIP1_HUMAN]
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Human glioma pathogenesis-related protein 1 (GLIPR1) is a membrane protein that is highly upregulated in brain cancers but is barely detectable in normal brain tissue. GLIPR1 is composed of a signal peptide that directs its secretion, a conserved cysteine-rich CAP (cysteine-rich secretory proteins, antigen 5 and pathogenesis-related 1 proteins) domain and a transmembrane domain. GLIPR1 is currently being investigated as a candidate for prostate cancer gene therapy and for glioblastoma targeted therapy. Crystal structures of a truncated soluble domain of the human GLIPR1 protein (sGLIPR1) solved by molecular replacement using a truncated polyalanine search model of the CAP domain of stecrisp, a snake-venom cysteine-rich secretory protein (CRISP), are presented. The correct molecular-replacement solution could only be obtained by removing all loops from the search model. The native structure was refined to 1.85 A resolution and that of a Zn(2+) complex was refined to 2.2 A resolution. The latter structure revealed that the putative binding cavity coordinates Zn(2+) similarly to snake-venom CRISPs, which are involved in Zn(2+)-dependent mechanisms of inflammatory modulation. Both sGLIPR1 structures have extensive flexible loop/turn regions and unique charge distributions that were not observed in any of the previously reported CAP protein structures. A model is also proposed for the structure of full-length membrane-bound GLIPR1.
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Structural studies of human glioma pathogenesis-related protein 1.,Asojo OA, Koski RA, Bonafe N Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):847-55. Epub 2011, Sep 8. PMID:21931216<ref>PMID:21931216</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 3q2u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Asojo, O A]]
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[[Category: Asojo OA]]
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[[Category: Crisp]]
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[[Category: Membrane protein]]
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[[Category: Rtvp1]]
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Revision as of 11:31, 14 March 2024

Structure of Human Glioma Pathogenesis-related Protein 1 Reveals Unique loops and surface motifs.

PDB ID 3q2u

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