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The site is oblong and runs along a flat ridge on the upper half of domain 1, which is proposed to dock to a groove in the I domain of LFA-1, with the critical Glu-37 residue ligating the Mg\n                    <jats:sup>2+<\/jats:sup>\n                    in the I domain. Previous mutagenesis of ICAM-1 and ICAM-3, interpreted in light of the recently determined ICAM-1 and ICAM-2 structures, suggests similar binding sites. By contrast, major differences are seen with vascular cell adhesion molecule-1 (VCAM-1), which binds \u03b1\n                    <jats:sub>4<\/jats:sub>\n                    integrins that lack an I domain. The binding site on VCAM-1 includes the lower portion of domain 1 and the upper part of domain 2, whereas the LFA-1 binding site on ICAM is confined to the upper part of domain 1.\n                  <\/jats:p>","DOI":"10.1073\/pnas.96.6.3017","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:39:15Z","timestamp":1027679955000},"page":"3017-3022","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":25,"title":["Lymphocyte function-associated antigen-1 binding residues in intercellular adhesion molecule-2 (ICAM-2) and the integrin binding surface in the ICAM subfamily"],"prefix":"10.1073","volume":"96","author":[{"given":"Jos\u00e9 M.","family":"Casasnovas","sequence":"first","affiliation":[{"name":"The Center for Blood Research and Harvard Medical School, Department of Pathology, 200 Longwood Avenue, Boston, MA 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