2tnf: Difference between revisions

Revision as of 12:52, 27 July 2008

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File:2tnf.png

Template:STRUCTURE 2tnf

1.4 A RESOLUTION STRUCTURE OF MOUSE TUMOR NECROSIS FACTOR, TOWARDS MODULATION OF ITS SELCTIVITY AND TRIMERISATION1.4 A RESOLUTION STRUCTURE OF MOUSE TUMOR NECROSIS FACTOR, TOWARDS MODULATION OF ITS SELCTIVITY AND TRIMERISATION

Template:ABSTRACT PUBMED 10089307

About this StructureAbout this Structure

2TNF is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The structure of mouse tumour-necrosis factor at 1.4 A resolution: towards modulation of its selectivity and trimerization., Baeyens KJ, De Bondt HL, Raeymaekers A, Fiers W, De Ranter CJ, Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):772-8. PMID:10089307

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OCA

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-'''1.4 A RESOLUTION STRUCTURE OF MOUSE TUMOR NECROSIS FACTOR, TOWARDS MODULATION OF ITS SELCTIVITY AND TRIMERISATION'''
+===1.4 A RESOLUTION STRUCTURE OF MOUSE TUMOR NECROSIS FACTOR, TOWARDS MODULATION OF ITS SELCTIVITY AND TRIMERISATION===
-==Overview==
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-The 1.4 A resolution structure of recombinant mouse tumour-necrosis factor alpha (mTNF) at 100 K has been determined. The crystals are triclinic, space group P1, with unit-cell parameters a = 48.06, b = 48.18, c = 51.01 A, alpha = 114.8, beta = 103.6, gamma = 91.1 degrees. The structure was refined to a final crystallographic R value of 19.7% (Rfree = 23.3%), including 3477 protein atoms, one 2-propanol molecule, one Tris molecule and 240 water molecules. Throughout the crystal lattice, the trimers are differently packed compared with human TNF, which was crystallized in the tetragonal space group P41212 and refined to 2.6 A resolution. The structures of mTNF and human TNF are very similar, diverging mainly in regions that are either flexible and/or involved in crystal packing. Some loops in mTNF which contain residues important for receptor binding are better resolved than in human TNF, such as the surface-exposed loops 30-34 and 144-147, which are also important for receptor specificity. Compared with human TNFs, the channel formed by the three monomers in mTNF is narrower. One 2-propanol molecule trapped in the trimeric channel could be a lead compound for the design of TNF inhibitors.
+The line below this paragraph, {{ABSTRACT_PUBMED_10089307}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Signal-anchor]]
 [[Category: Transmembrane]]
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