Related ArticlesNMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Feb 4;275(5):3264-9
Authors: Dolmer K, Huang W, Gettins PG
We have used NMR methods to determine the structure of the calcium complex of complement-like repeat 3 (CR3) from the low density lipoprotein receptor-related protein (LRP) and to examine its specific interaction with the receptor binding domain of human alpha(2)-macroglobulin. CR3 is one of eight related repeats that constitute a major ligand binding region of LRP. The structure is very similar in overall fold to homologous complement-like repeat CR8 from LRP and complement-like repeats LB1, LB2, and LB5 from the low density lipoprotein receptor and contains a short two-strand antiparallel beta-sheet, a one turn alpha-helix, and a high affinity calcium site with coordination from four carboxyls and two backbone carbonyls. The surface electrostatics and topography are, however, quite distinct from each of these other repeats. Two-dimensional (1)H,(15)N-heteronuclear single quantum coherence spectra provide evidence for a specific, though relatively weak (K(d) approximately 140 microM), interaction between CR3 and human alpha2-macroglobulin receptor binding domain that involves a contiguous patch of surface residues in the central region of CR3. This specific interaction is consistent with a mode of LRP binding to ligands that uses contributions from more than one domain to generate a wide array of different binding sites, each with overall high affinity.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
J Struct Funct Genomics. 2010 Dec 14;
Authors: Mani R, Vorobiev S, Swapna GV, Neely H, Janjua H, Ciccosanti C, Xiao R, Acton TB, Everett JK, Hunt J, Montelione GT
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural...
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[NMR paper] NMR studies of lipoprotein structure.
NMR studies of lipoprotein structure.
Related Articles NMR studies of lipoprotein structure.
Annu Rev Biophys Biomol Struct. 2002;31:177-206
Authors: Cushley RJ, Okon M
Early NMR structural studies of serum lipoproteins were based on (1)H, (13)C, (31)P, and (2)H studies of lipid components. From the early studies information on composition, lipid chain dynamics and order parameters, and monolayer organization resulted. More recently, selective or complete isotopic labeling techniques, combined with multidimensional NMR spectroscopy, have...
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[NMR paper] NMR studies of a viral protein that mimics the regulators of complement activation.
NMR studies of a viral protein that mimics the regulators of complement activation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of a viral protein that mimics the regulators of complement activation.
J Mol Biol. 1997 Sep 19;272(2):253-65
Authors: Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN
Vaccinia virus complement control protein (VCP) is a 243-residue protein that is similar in sequence to the regulators of complement activation; its...
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[NMR paper] Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Biochemistry. 1996 Jan 23;35(3):698-703
Authors: Butcher DJ, Nedved ML, Neiss TG, Moe GR
The structure of a 22 amino acid peptide, TPPI , that is similar to the proline repeat segment of the replication arrest protein, Tus, has been determined by 1H NMR in 50% trifluroethanol. The...
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[NMR paper] Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Related Articles Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Biochemistry. 1991 Jan 29;30(4):997-1004
Authors: Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID
The complement control protein (CCP) module (also known as the short consensus repeat) is a consensus sequence of about 60 amino acid residues which is thought to fold independently. It occurs over 140 times in more than 20 extracellular...
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[NMR paper] Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the
Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Related Articles Dynamic structure of the lower density lipoproteins. II. Deuterium NMR studies of the monolayer of very low and low density lipoproteins.
Biochem Cell Biol. 1990 Jan;68(1):189-98
Authors: Chana RS, Treleaven WD, Parmar YI, Cushley RJ
The order of phosphatidylcholine (PC) acyl chains in the surface monolayer of very low density lipoproteins (VLDL) and low density lipoproteins (LDL) has been...
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[NMR paper] NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Related Articles NMR analysis of low-density lipoprotein oxidatively-modified in vitro.
Free Radic Res Commun. 1990;8(3):175-83
Authors: Barenghi L, Bradamante S, Giudici GA, Vergani C
Human plasma low density lipoprotein has been oxidized at different stages in vitro and analysed by 1H, 13C, and 31P NMR spectroscopy and by biochemical methods. Information was obtained on: a) structure mobilities of lipids and on lipid-protein interactions; b) conjugated and oxo-dienes; c)...
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[NMR paper] NMR solution structure of complement-like repeat CR8 from the low density lipoprotein
NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.
J Biol Chem. 1999 May 14;274(20):14130-6
Authors: Huang W, Dolmer K, Gettins PG
The low density lipoprotein receptor-related protein is a member of the low density...
NMR solution structure of complement-like repeat CR3 from the low density lipoprotein
Linear Mode
