{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T08:37:22Z","timestamp":1790757442701,"version":"4.1.0"},"reference-count":64,"publisher":"American Chemical Society (ACS)","issue":"28","license":[{"start":{"date-parts":[[2015,7,9]],"date-time":"2015-07-09T00:00:00Z","timestamp":1436400000000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM49758"],"award-info":[{"award-number":["GM49758"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,7,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The X-ray crystal structure of arginase from Schistosoma mansoni (SmARG) and the structures of its complexes with several amino acid inhibitors have been determined at atomic resolution. SmARG is a binuclear manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to form l-ornithine and urea, and this enzyme is upregulated in all forms of the parasite that interact with the human host. Current hypotheses suggest that parasitic arginases could play a role in host immune evasion by depleting pools of substrate l-arginine that would otherwise be utilized for NO biosynthesis and NO-dependent processes in the immune response. Although the amino acid sequence of SmARG is only 42% identical with that of human arginase I, residues important for substrate binding and catalysis are strictly conserved. In general, classical amino acid inhibitors such as 2(S)-amino-6-boronohexanoic acid (ABH) tend to bind more weakly to SmARG than to human arginase I despite identical inhibitor binding modes in each enzyme active site. The identification of a patch on the enzyme surface capable of accommodating the additional C\u03b1 substitutent of an \u03b1,\u03b1-disubstituted amino acid inhibitor suggests that such inhibitors could exhibit higher affinity and biological activity. The structures of SmARG complexed with two different \u03b1,\u03b1-disubstituted derivatives of ABH are presented and provide a proof of concept for this approach in the enhancement of enzyme\u2013inhibitor affinity.<\/jats:p>","DOI":"10.1021\/bi5004519","type":"journal-article","created":{"date-parts":[[2014,7,9]],"date-time":"2014-07-09T10:23:24Z","timestamp":1404901404000},"page":"4671-4684","source":"Crossref","is-referenced-by-count":22,"title":["Crystal Structure of\n                    <i>Schistosoma mansoni<\/i>\n                    Arginase, a Potential Drug Target for the Treatment of Schistosomiasis"],"prefix":"10.1021","volume":"53","author":[{"given":"Yang","family":"Hai","sequence":"first","affiliation":[{"name":"University of Pennsylvania , , , ,","place":["Philadelphia, Pennsylvania, United States, 19104-6323"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer E.","family":"Edwards","sequence":"additional","affiliation":[{"name":"Aberystwyth University , , , ,","place":["Aberystwyth, Ceredigion, United Kingdom, SY23 3DA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael C.","family":"Van Zandt","sequence":"additional","affiliation":[{"name":"New England Discovery Partners , 23 Business Park Drive , , ,","place":["Branford, Connecticut, United States, 06405"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karl F.","family":"Hoffmann","sequence":"additional","affiliation":[{"name":"Aberystwyth University , , , ,","place":["Aberystwyth, Ceredigion, United Kingdom, SY23 3DA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David W.","family":"Christianson","sequence":"additional","affiliation":[{"name":"University of Pennsylvania , , , ,","place":["Philadelphia, Pennsylvania, United States, 19104-6323"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,7,9]]},"reference":[{"issue":"2","key":"2026090400210242000_cit1","doi-asserted-by":"crossref","first-page":"e1475","DOI":"10.1371\/journal.pntd.0001475","article-title":"Neglected\ntropical diseases of the\nMiddle East and North Africa: Review of their prevalence, distribution,\nand opportunities for control","volume":"6","author":"Hotez","year":"2012","journal-title":"PLoS Neglected\nTrop. 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