Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations

Journal of Biological Chemistry

Volumn 283, Issue 14, 2008, Pages 9475-9487

  Hocking, Henry G ^a   Herbert, Andrew P ^a   Kavanagh, David ^a   Soares, Dinesh C ^a   Ferreira, Viviana P ^b   Pangburn, Michael K ^b   Uhrín, Dušan ^a   Barlow, Paul N ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b UNIVERSITY OF TEXAS HEALTH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL CULTURE; HUMAN ENGINEERING; NUCLEAR MAGNETIC RESONANCE; NUCLEIC ACIDS;

ACCELERATING FACTORS; BACKBONE STRUCTURES; COFACTOR ACTIVITIES; COMPLEMENT CONTROL PROTEIN MODULES; COMPLEMENT RECEPTOR TYPE 1; COMPLEMENT SYSTEMS; FUNCTIONAL SITES; HIGHER TEMPERATURES; HUMAN FACTOR H; MACULAR DEGENERATIONS; MINIMAL UNITS; MOLECULAR SURFACES; SEQUENCE VARIATIONS; SINGLE NUCLEOTIDES; STRUCTURAL CHANGES; STRUCTURAL COMPARISONS; TERMINAL REGIONS; THERMAL STABILITIES; TWIST ANGLES;

PORT TERMINALS;

ARGININE; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3B RECEPTOR; COMPLEMENT FACTOR H; HISTIDINE; ISOLEUCINE; VALINE; ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT FACTOR H, HUMAN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; HEMOLYTIC UREMIC SYNDROME; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; RETINA MACULA AGE RELATED DEGENERATION; SINGLE NUCLEOTIDE POLYMORPHISM; THERMOSTABILITY; AMINO ACID SUBSTITUTION; CHEMISTRY; GENETIC DISORDER; GENETICS; HUMAN; KIDNEY DISEASE; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN TERTIARY STRUCTURE;

AMINO ACID SUBSTITUTION; COMPLEMENT C3B; COMPLEMENT FACTOR B; COMPLEMENT FACTOR H; GENETIC DISEASES, INBORN; HUMANS; KIDNEY DISEASES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; POLYMORPHISM, SINGLE NUCLEOTIDE; PROTEIN STRUCTURE, TERTIARY;

EID: 44049086967     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M709587200     Document Type: Article

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