1n1i

<table><tr><td colspan='2'>[[1n1i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plakh Plakh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N1I FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1b9w|1b9w]], [[1cej|1cej]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5851 PLAKH])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1i OCA], [http://pdbe.org/1n1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n1i RCSB], [http://www.ebi.ac.uk/pdbsum/1n1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1i ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The protozoan parasite Plasmodium causes malaria, with hundreds of millions of cases recorded annually. Protection against malaria infection can be conferred by antibodies against merozoite surface protein (MSP)-1, making it an attractive vaccine candidate. Here we present the structure of the C-terminal domains of MSP-1 (known as MSP-1(19)) from Plasmodium knowlesi. The structure reveals two tightly packed epidermal growth factor-like domains oriented head to tail. In domain 1, the molecule displays a histidine binding site formed primarily by a highly conserved tryptophan. The protein carries a pronounced overall negative charge primarily due to the large number of acidic groups in domain 2. To map protein binding surfaces on MSP-1(19), we have analyzed the crystal contacts in five different crystal environments, revealing that domain 1 is highly preferred in protein-protein interactions. A comparison of MSP-1(19) structures from P. knowlesi, P. cynomolgi, and P. falciparum shows that, although the overall protein folds are similar, the molecules show significant differences in charge distribution. We propose the histidine binding site in domain 1 as a target for inhibitors of protein binding to MSP-1, which might prevent invasion of the merozoite into red blood cells.

Structure of the C-terminal domains of merozoite surface protein-1 from Plasmodium knowlesi reveals a novel histidine binding site.,Garman SC, Simcoke WN, Stowers AW, Garboczi DN J Biol Chem. 2003 Feb 28;278(9):7264-9. Epub 2002 Dec 19. PMID:12493733<ref>PMID:12493733</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1n1i" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Plakh]]

[[Category: Garboczi, D N]]

[[Category: Garman, S C]]

[[Category: Simcoke, W N]]

[[Category: Stowers, A W]]

[[Category: Surface protein]]