1dok

MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM

spinqualitylabelsall models 1dok, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dok is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CCL2_HUMAN Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The X-ray crystal structure of recombinant human monocyte chemoattractant protein (MCP-1) has been solved in two crystal forms. One crystal form (P), refined to 1.85 A resolution, contains a dimer in the asymmetric unit, while the other (I) contains a monomer and was refined at 2.4 A. Although both crystal forms grow together in the same droplet, the respective quaternary structures of the protein differ dramatically. In addition, both X-ray structures differ to a similar extent from the solution structure of MCP-1. Such extent of variability of quaternary structures is unprecedented. In the crystal structures, the well-ordered N termini of MCP-1 form 3(10)-helices. Comparison of the three MCP-1 structures revealed a direct correlation between the main-chain conformation of the first two cysteine residues and the quaternary arrangements. These data can be used to explain the structural basis for the assignment of residues responsible for biological activity. The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions.,Lubkowski J, Bujacz G, Boque L, Domaille PJ, Handel TM, Wlodawer A Nat Struct Biol. 1997 Jan;4(1):64-9. PMID:8989326 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monocyte chemoattractant protein

Proteopedia Page Contributors and Editors (what is this?)

OCA