2afp | pdb_00002afp

THE SOLUTION STRUCTURE OF TYPE II ANTIFREEZE PROTEIN REVEALS A NEW MEMBER OF THE LECTIN FAMILY

spinqualitylabelsall models 2afp, 5 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2afp is a 1 chain structure with sequence from Hemam. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ISP2_HEMAM] Antifreeze proteins lower the blood freezing point. 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 A recombinant form of the sea raven type II antifreeze protein (SRAFP) has been produced using the Pichia pastoris expression system. The antifreeze activity of recombinant SRAFP is indistinguishable from that of the wild-type protein. The global fold of SRAFP has been determined by two-dimensional 1H homonuclear and three-dimensional 1H- inverted question mark15N inverted question mark heteronuclear NMR spectroscopy using 785 NOE distance restraints and 47 angular restraints. The molecule folds into one globular domain that consists of two helices and nine beta-strands in two beta-sheets. The structure confirms the proposed existence of five disulfide bonds. The global fold of SRAFP is homologous to C-type lectins and pancreatic stone proteins, even though the sequence identity is only approximately 20%. The solution structure of type II antifreeze protein reveals a new member of the lectin family.,Gronwald W, Loewen MC, Lix B, Daugulis AJ, Sonnichsen FD, Davies PL, Sykes BD Biochemistry. 1998 Apr 7;37(14):4712-21. PMID:9537986 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antifreeze protein

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