The immunoglobulin (Ig) superfamily is one of the largest families in the vertebrate genome, found most frequently in cell surface molecules. Intercellular adhesion molecule-1 (ICAM-1) contains five extracellular Ig superfamily domains (D1-D5) of which the first domain, D1, is the binding site for the integrin lymphocyte function-associated antigen-1 (LFA-1) and human rhinovirus. Despite the modular nature of many Ig superfamily domains with respect to domain folding and ligand recognition, D1 does not fold on its own due to the loss of its interaction with the second domain. The goal of this study was to engineer ICAM-1 D1 by introducing mutations that would stabilize the Ig superfamily domain fold while retaining its ability to bind to LFA-1 and rhinovirus. First, with a directed evolution approach, we isolated mutations in D1 that showed binding to conformation-specific antibodies and the ligand binding domain of LFA-1 called the inserted, or I, domain. Then, with a rational design approach we introduced mutations that contributed to the stability of ICAM-1 D1 in solution. The mutations that restored native folding of D1 in isolation were those that would convert hydrogen bond networks in buried regions into hydrophobic contacts. Notably, for most mutations, identical or similar types of substitutions were found in ICAM-1 molecules of different species and other ICAM family members. The systematic approach demonstrated in this study to engineer a single Ig superfamily fold in ICAM-1 can be broadly applicable to the engineering of modular Ig superfamily domains in other cell surface molecules.Intercellular adhesion molecule-1 (ICAM-1) 4 is an inducible transmembrane receptor expressed on the surface of several cell types including leukocytes and endothelial cells and is up-regulated by inflammatory mediators such as interleukin-1, interferon-␥, tumor necrosis factor, and lipopolysaccharide (1). ICAM-1 is the counter receptor for the leukocyte integrins, lymphocyte function-associated antigen-1 (LFA-1, ␣ L ␤ 2 ), Mac-1 (␣ M ␤ 2 ), and p150,95 (␣ x ␤ 2 ), and promotes cellular interactions important in immunity and inflammation (2-7). ICAM-1 is also used as a sequestration receptor for Plasmodium falciparum-infected erythrocytes (8) and has been subverted as a receptor for human rhinovirus (9, 10) and Coxsackievirus A21 (11). Structurally, ICAM-1 consists of five extracellular domains (D1-D5), a transmembrane spanning region, and a short cytoplasmic domain. The second, third, and fourth domains of ICAM-1 contain a number of glycan chains that appear to contribute to ICAM-1 stability and function (12-14). All five extracellular domains of ICAM-1 belong to the immunoglobulin (Ig) superfamily, a family that is the largest in the vertebrate genome (15) and found in many cell surface receptors (16). Ig superfamily domains frequently exist in tandem arrays in surface receptors, and each domain in one molecule may pair with different ligands.The Ig superfamily fold is characterized by a ␤-sandwich structure consisting ...

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Objectives The purpose of this study is to give account of effects of the Korean herbal medicine therapy which is based on the Sasang constitutional medicine for the patient who has suffered from scale of back caused by psoriasis. Method Psoriasis patient was diagnosed Soeumin based on his nature and emotion, physical characteristics, symptoms. He was medicated Soeumin Goepungsan. Results and Conclusions Psoriasis patient who was treated with Soeumin Goepoong-san showed improvement in Psoriasis symptom and general condition. This case study describes the effectiveness on psoriasis symptom by using Soeumin Goepoong-san.

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