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<StructureSection load='1bih' size='340' side='right'caption='[[1bih]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='1bih' size='340' side='right'caption='[[1bih]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cecropia_moth Cecropia moth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyalophora_cecropia Hyalophora cecropia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1bih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bih OCA], [https://pdbe.org/1bih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bih RCSB], [https://www.ebi.ac.uk/pdbsum/1bih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bih 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=1bih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bih OCA], [https://pdbe.org/1bih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bih RCSB], [https://www.ebi.ac.uk/pdbsum/1bih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bih ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/HEMO_HYACE HEMO_HYACE]] Insect-immune protein. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.  
[https://www.uniprot.org/uniprot/HEMO_HYACE HEMO_HYACE] Insect-immune protein. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1bih ConSurf].
</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=1bih ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hemolin, an insect immunoglobulin superfamily member, is a lipopolysaccharide-binding immune protein induced during bacterial infection. The 3.1 angstrom crystal structure reveals a bound phosphate and patches of positive charge, which may represent the lipopolysaccharide binding site, and a new and unexpected arrangement of four immunoglobulin-like domains forming a horseshoe. Sequence analysis and analytical ultracentrifugation suggest that the domain arrangement is a feature of the L1 family of neural cell adhesion molecules related to hemolin. These results are relevant to interpretation of human L1 mutations in neurological diseases and suggest a domain swapping model for how L1 family proteins mediate homophilic adhesion.
Crystal structure of hemolin: a horseshoe shape with implications for homophilic adhesion.,Su XD, Gastinel LN, Vaughn DE, Faye I, Poon P, Bjorkman PJ Science. 1998 Aug 14;281(5379):991-5. PMID:9703515<ref>PMID:9703515</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1bih" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cecropia moth]]
[[Category: Hyalophora cecropia]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bjorkman, P J]]
[[Category: Bjorkman PJ]]
[[Category: Faye, I]]
[[Category: Faye I]]
[[Category: Gastinel, L N]]
[[Category: Gastinel LN]]
[[Category: Poon, P]]
[[Category: Poon P]]
[[Category: Su, X D]]
[[Category: Su X-D]]
[[Category: Vaughn, D E]]
[[Category: Vaughn DE]]
[[Category: Homophilic adhesion]]
[[Category: Insect immunity]]
[[Category: Lps-binding]]

Latest revision as of 15:33, 13 March 2024

CRYSTAL STRUCTURE OF THE INSECT IMMUNE PROTEIN HEMOLIN: A NEW DOMAIN ARRANGEMENT WITH IMPLICATIONS FOR HOMOPHILIC ADHESION

1bih, resolution 3.10Å

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