Query author contributions in Reactome
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Details on Person Human CRP binds with highest affinity to phosphocholine resi...
| Class:Id | Summation:976793 |
|---|---|
| _displayName | Human CRP binds with highest affinity to phosphocholine resi... |
| _timestamp | 2010-10-13 16:29:47 |
| created | [InstanceEdit:976791] Jupe, S, 2010-10-13 |
| literatureReference | [LiteratureReference:976794] C-reactive protein: binding to lipids and lipoproteins [LiteratureReference:976756] Interaction of C-reactive protein with artificial phosphatidylcholine bilayers [LiteratureReference:976813] Complement activation by C-reactive protein complexes [LiteratureReference:976735] Regulation of complement activation by C-reactive protein [LiteratureReference:976726] C-reactive Protein |
| text | Human CRP binds with highest affinity to phosphocholine residues, but also binds a variety of other autologous and extrinsic ligands (Black et al. 2004), leading to aggregation of the structures bearing these ligands. Calcium is required for binding to occur. Autologous ligands include native and modified plasma lipoproteins (Pepys et al. 1985), damaged cell membranes (Volanakis & Wirtz 1979), various phospholipids and related compounds, and apoptotic cells (Gershov et al. 2000). Extrinsic ligands include many glycan, phospholipid, and other constituents of microorganisms, such as capsular and somatic components of bacteria, fungi, and parasites. When aggregated or bound to macromolecular ligands, human CRP is recognized by C1q and potently activates the classical complement pathway, engaging C3, the main adhesion molecule of the complement system, and the terminal membrane attack complex, C5–C9 (Volanakis 1982, Mold et al. 1999). |
| (summation) | [Reaction:976766] C-reactive protein pentamers bind microbial phosphocholines [Homo sapiens] |
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