1bih

<StructureSection load='1bih' size='340' side='right' caption='[[1bih]], [[Resolution|resolution]] 3.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[1bih]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BIH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bih RCSB], [http://www.ebi.ac.uk/pdbsum/1bih PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/HEMO_HYACE HEMO_HYACE]] Insect-immune protein. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bi/1bih_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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== References ==

<references/>

[[Category: Bjorkman, P J]]

[[Category: Faye, I]]

[[Category: Gastinel, L N]]

[[Category: Poon, P]]

[[Category: Su, X D]]

[[Category: Vaughn, D E]]

[[Category: Lps-binding]]