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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2001-6-20
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pubmed:abstractText |
In this review we summarise more than 10 years of biophysical exploration into the structural biology of the regulators of complement activation (RCA). The five human proteins responsible for regulation of the early events of complement are homologous and are composed largely from building blocks called "complement control protein (CCP) modules". Unlike most multiple domain proteins they do not contain any of the other widely occurring module types. This apparent simplicity of RCA structure, however, is belied by their sophistication of function. In fact, the structures of the individual CCP modules exhibit wide variations on a common theme while the extent and nature of intermodular connections is diverse. Some neighbouring modules within a protein stabilise each other and some co-operate to form specific binding surfaces. The degree of true "modularity" of CCPs is open to debate. The study of RCA proteins clearly illustrates the value of combining complementary structural biology techniques. The results could have implications for folding, evolution, flexibility and structure-function relationships of other molecules in the large, diverse and little understood category of multiple domain proteins.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD46,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD55,
http://linkedlifedata.com/resource/pubmed/chemical/CD46 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Factor B,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Factor H,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alphaXbeta2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement 3b,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Complement 3d,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/complement factor H, human,
http://linkedlifedata.com/resource/pubmed/chemical/complement-control protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0105-2896
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
180
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
146-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11414356-Amino Acid Motifs,
pubmed-meshheading:11414356-Amino Acid Sequence,
pubmed-meshheading:11414356-Antigens, CD,
pubmed-meshheading:11414356-Antigens, CD46,
pubmed-meshheading:11414356-Antigens, CD55,
pubmed-meshheading:11414356-Complement Activation,
pubmed-meshheading:11414356-Complement Factor B,
pubmed-meshheading:11414356-Complement Factor H,
pubmed-meshheading:11414356-Consensus Sequence,
pubmed-meshheading:11414356-Humans,
pubmed-meshheading:11414356-Integrin alphaXbeta2,
pubmed-meshheading:11414356-Magnetic Resonance Spectroscopy,
pubmed-meshheading:11414356-Membrane Glycoproteins,
pubmed-meshheading:11414356-Models, Molecular,
pubmed-meshheading:11414356-Molecular Sequence Data,
pubmed-meshheading:11414356-Protein Binding,
pubmed-meshheading:11414356-Protein Conformation,
pubmed-meshheading:11414356-Protein Structure, Tertiary,
pubmed-meshheading:11414356-Receptors, Complement 3b,
pubmed-meshheading:11414356-Receptors, Complement 3d,
pubmed-meshheading:11414356-Sequence Alignment,
pubmed-meshheading:11414356-Sequence Homology, Amino Acid,
pubmed-meshheading:11414356-Structure-Activity Relationship,
pubmed-meshheading:11414356-Viral Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
Structure and flexibility of the multiple domain proteins that regulate complement activation.
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pubmed:affiliation |
Center for Neurological Diseases, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts, USA.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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