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Volumn 99, Issue 10, 2002, Pages 6607-6612
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The 1.9-Å crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link
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Author keywords
[No Author keywords available]
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Indexed keywords
COLLAGEN TYPE 4;
LYSINE;
METHIONINE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CROSS LINKING;
CRYSTAL STRUCTURE;
CRYSTALLIZATION;
DIFFRACTION;
HUMAN;
HUMAN TISSUE;
PLACENTA;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN PROTEIN INTERACTION;
PROTEIN STABILITY;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
CHEMICAL STRUCTURE;
CHEMISTRY;
FEMALE;
GENETICS;
METABOLISM;
MOLECULAR GENETICS;
PROTEIN CONFORMATION;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE HOMOLOGY;
X RAY CRYSTALLOGRAPHY;
AMINO ACID SEQUENCE;
COLLAGEN TYPE IV;
CRYSTALLOGRAPHY, X-RAY;
FEMALE;
HUMANS;
LYSINE;
METHIONINE;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MOLECULAR STRUCTURE;
PLACENTA;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
SEQUENCE HOMOLOGY, AMINO ACID;
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EID: 18344390410
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.062183499 Document Type: Article |
Times cited : (112)
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References (34)
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