1nap
From Proteopedia
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| - | [[Image:1nap.jpg|left|200px]] | + | [[Image:1nap.jpg|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN NEUTROPHIL-ACTIVATING PEPTIDE-2 (M6L) AT 1.9-ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1nap |SIZE=350|CAPTION= <scene name='initialview01'>1nap</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN NEUTROPHIL-ACTIVATING PEPTIDE-2 (M6L) AT 1.9-ANGSTROMS RESOLUTION''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NAP is a [ | + | 1NAP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7706245 7706245] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytokine]] | [[Category: cytokine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:24 2008'' |
Revision as of 10:54, 20 March 2008
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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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