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1nap

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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Edwards, B.F.P.]]
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[[Category: Edwards, B F.P.]]
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[[Category: Malkowski, M.G.]]
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[[Category: Malkowski, M G.]]
[[Category: cytokine]]
[[Category: cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:27:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:06 2008''

Revision as of 12:04, 21 February 2008


1nap, resolution 1.9Å

Drag the structure with the mouse to rotate

THE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN NEUTROPHIL-ACTIVATING PEPTIDE-2 (M6L) AT 1.9-ANGSTROMS RESOLUTION

Overview

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.

About this Structure

1NAP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9-A resolution., Malkowski MG, Wu JY, Lazar JB, Johnson PH, Edwards BF, J Biol Chem. 1995 Mar 31;270(13):7077-87. PMID:7706245

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