The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions

Nature Structural Biology

Volumn 4, Issue 1, 1997, Pages 64-69

  Lubkowski, Jacek ^a   Bujacz, Grzegorz ^a,d   Boqué, Lluís ^a   Domaille, Peter J ^b   Handel, Tracy M ^c   Wlodawer, Alexander ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b DUPONT COMPANY   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MONOCYTE CHEMOTACTIC PROTEIN 1; MONOMER; RECOMBINANT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; DIMERIZATION; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STEREOCHEMISTRY; X RAY CRYSTALLOGRAPHY;

BIOPOLYMERS; CHEMOKINE CCL2; CRYSTALLOGRAPHY, X-RAY; HUMANS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS;

EID: 0031026207     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0197-64     Document Type: Article

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