Pathophysiological condition changes the conformation of a flexible FBG-related protein, switching it from pathogen-recognition to host-interaction

Biochimie

Volumn 93, Issue 10, 2011, Pages 1710-1719

  Zhang, Jing ^a   Yang, Lifeng ^a,b   Anand, Ganesh Srinivasan ^a   Ho, Bow ^c   Ding, Jeak Ling ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b SINGAPORE MIT ALLIANCE   (Singapore)

^c NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

C reactive protein (CRP); Conformational change; Fibrinogen like domain (FBG); Fibrinogen related protein (FREP); Hydrogen deuterium exchange mass spectrometry (HDMS)

Indexed keywords

BINDING PROTEIN; C REACTIVE PROTEIN; CALCIUM; FIBRINOGEN; FIBRINOGEN RELATED PROTEIN; FICOLIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; HOST PATHOGEN INTERACTION; HUMAN; MASS SPECTROMETRY; NONHUMAN; PATHOPHYSIOLOGY; PH; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS;

C-REACTIVE PROTEIN; CELL LINE; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; LECTINS; MASS SPECTROMETRY; MUTAGENESIS, SITE-DIRECTED; PHYLOGENY; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SURFACE PLASMON RESONANCE;

EID: 80052099312     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.06.003     Document Type: Article

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