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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
13
|
| pubmed:dateCreated |
1995-5-10
|
| pubmed:abstractText |
Neutrophil-activating peptide-2 (NAP-2) is a 70-residue carboxyl-terminal fragment of platelet basic protein, which is found in the alpha-granules of human platelets. NAP-2, which belongs to the CXC family of chemokines that includes interleukin-8 and platelet factor 4, binds to the interleukin-8 type II receptor and induces a rise in cytosolic calcium, chemotaxis of neutrophils, and exocytosis. Crystals of recombinant NAP-2 in which the single methionine at position 6 was replaced by leucine to facilitate expression belong to space group P1 (unit cell parameters a = 40.8, b = 43.8, and c = 44.7 A and alpha = 98.4 degrees, beta = 120.3 degrees, and gamma = 92.8 degrees), with 4 molecules of NAP-2 (Mr = 7600) in the asymmetric unit. The molecular replacement solution calculated with bovine platelet factor 4 as the starting model was refined using rigid body refinement, manual fitting in solvent-leveled electron density maps, simulated annealing, and restrained least squares to an R-factor of 0.188 for 2 sigma data between 7.0- and 1.9-A resolution. The final refined crystal structure includes 265 solvent molecules. The overall tertiary structure, which is similar to that of platelet factor 4 and interleukin-8, includes an extended amino-terminal loop, three strands of antiparallel beta-sheet arranged in a Greek key fold, and one alpha-helix at the carboxyl terminus. The Glu-Leu-Arg sequence that is critical for receptor binding is fully defined by electron density and exhibits multiple conformations.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-8,
http://linkedlifedata.com/resource/pubmed/chemical/PPBP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Factor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Thromboglobulin,
http://linkedlifedata.com/resource/pubmed/chemical/connective tissue-activating peptide
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
31
|
| pubmed:volume |
270
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
7077-87
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7706245-Amino Acid Sequence,
pubmed-meshheading:7706245-Cloning, Molecular,
pubmed-meshheading:7706245-Crystallography, X-Ray,
pubmed-meshheading:7706245-Escherichia coli,
pubmed-meshheading:7706245-Humans,
pubmed-meshheading:7706245-Hydrogen Bonding,
pubmed-meshheading:7706245-Interleukin-8,
pubmed-meshheading:7706245-Models, Molecular,
pubmed-meshheading:7706245-Molecular Sequence Data,
pubmed-meshheading:7706245-Neutrophils,
pubmed-meshheading:7706245-Peptides,
pubmed-meshheading:7706245-Platelet Factor 4,
pubmed-meshheading:7706245-Protein Conformation,
pubmed-meshheading:7706245-Protein Structure, Secondary,
pubmed-meshheading:7706245-Protein Structure, Tertiary,
pubmed-meshheading:7706245-Recombinant Proteins,
pubmed-meshheading:7706245-Sequence Homology, Amino Acid,
pubmed-meshheading:7706245-beta-Thromboglobulin
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution.
|
| pubmed:affiliation |
Department of Biochemistry, Wayne State University, Detroit, Michigan 48201, USA.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|