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| Untersuchte Arbeit: Seite: 19, Zeilen: 1-3 |
Quelle: Wright 2005 Seite(n): 59, 60, Zeilen: 59:right col. 50-54; 60: figure 2 |
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| The collectins are assembled as trimeric subunits, which multimerize to varying degrees. SP-A is mainly an octadecamer and forms a bouquet-like structure that is similar to MBL, whereas SP-D forms a dodecamer (Wright, 2005).
Figure 3: Collectin and C1q structure. Surfactant protein A (SP-A) and SP-D are members of a family of proteins known as collectins. a Collectins have collagen-like amino (N)-terminal regions and C-type (calcium dependent) carbohydrate-recognition domains (CRDs). Collectins consist of structural subunits that are composed of trimeric polypeptide chains, which are identical except for human SP-A. The trimers are assembled into oligomers. b SP-A and mannose-binding lectin (MBL) are octadecamers (18-mers), consisting of six trimeric subunits. SP-D is a dodecamer (12-mer), consisting of four trimeric subunits. Although C1q is structurally homologous to SP-A and MBL, it is not a collectin as it does not have a lectin domain (CRD) (adapted from Wright, 2005). Wright JR. Immunoregulatory functions of surfactant proteins. Nat Rev Immunol. 2005 Jan; 5 (1): 58-68. Review. |
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The collectins are assembled as trimeric subunits, which multimerize to varying degrees. SP-A is mainly an octadecamer and forms a bouquet-like structure that is similar to MBL, whereas SP-D forms a dodecamer (FIG. 2). [Page 60]
Figure 2 Collectin and C1q structure. Surfactant protein A (SP-A) and SP-D are members of a family of proteins known as collectins. a Collectins have collagen-like amino (N)-terminal regions and C-type (calcium dependent) carbohydrate-recognition domains (CRDs). Collectins consist of structural subunits that are composed of trimeric polypeptide chains, which are identical except for human SP-A. The trimers are assembled into oligomers. b SP-A and mannose-binding lectin (MBL) are octadecamers (18-mers), consisting of six trimeric subunits. SP-D is a dodecamer (12-mer), consisting of four trimeric subunits. Although C1q is structurally homologous to SP-A and MBL, it is not a collectin as it does not have a lectin domain (CRD). Note that these models are not drawn to scale. |
The source is mentioned. Nevertheless there is no hint that the texts are identical. The figure has not been "adapted" but rather "copied". |
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