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1pfm

From Proteopedia

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[[Image:1pfm.gif|left|200px]]
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{{STRUCTURE_1pfm| PDB=1pfm | SCENE= }}
{{STRUCTURE_1pfm| PDB=1pfm | SCENE= }}
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'''PF4-M2 CHIMERIC MUTANT WITH THE FIRST 10 N-TERMINAL RESIDUES OF R-PF4 REPLACED BY THE N-TERMINAL RESIDUES OF THE IL8 SEQUENCE. MODELS 1-15 OF A 27-MODEL SET.'''
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===PF4-M2 CHIMERIC MUTANT WITH THE FIRST 10 N-TERMINAL RESIDUES OF R-PF4 REPLACED BY THE N-TERMINAL RESIDUES OF THE IL8 SEQUENCE. MODELS 1-15 OF A 27-MODEL SET.===
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==Overview==
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Native human platelet factor 4 (PF4) is a homotetrameric protein (70 residues/subunit) known for its anticoagulant heparin binding activity. 2D 15N--1H HSQC NMR experiments of native PF4 in solution show the presence of conformational heterogeneity consistent with the formation of asymmetric homo-tetramers as observed in the X-ray crystal structure of both human and bovine PF4. A chimeric mutant of PF4 (called PF4-M2) which substitutes the first 11 N-terminal residues for the first eight residues from homologous interleukin-8 forms symmetric homo-tetramers with essentially the same heparin binding activity as native PF4. The solution structure of PF4-M2 has been investigated by using two- and three-dimensional 1H- and 15N-NMR spectroscopy and NOE-restrained simulated annealing molecular dynamics. As with other members of the CXC chemokine family whose structures are known, the PF4-M2 subunit monomer consists of a mostly hydrophobic, triple-stranded antiparallel beta-sheet onto which is folded an amphipathic C-terminal helix and a less periodic N-terminal domain. Although N-terminal substitution with the less acidic interleukin-8 sequence most affects the quarternary structure relative to native PF4 at the AC and AD dimer interfaces, AB dimer stability is weakened as reflected in reduced equilibrium association binding constants.
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(as it appears on PubMed at http://www.pubmed.gov), where 7547867 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7547867}}
==About this Structure==
==About this Structure==
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1PFM 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=1PFM OCA].
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1PFM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PFM OCA].
==Reference==
==Reference==
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[[Category: Rosa, G La.]]
[[Category: Rosa, G La.]]
[[Category: Cytokine]]
[[Category: Cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:01:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:56:11 2008''

Revision as of 10:56, 29 July 2008

Image:1pfm.png

Template:STRUCTURE 1pfm

PF4-M2 CHIMERIC MUTANT WITH THE FIRST 10 N-TERMINAL RESIDUES OF R-PF4 REPLACED BY THE N-TERMINAL RESIDUES OF THE IL8 SEQUENCE. MODELS 1-15 OF A 27-MODEL SET.

Template:ABSTRACT PUBMED 7547867

About this Structure

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

Reference

NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-terminal chimera: a symmetric tetramer., Mayo KH, Roongta V, Ilyina E, Milius R, Barker S, Quinlan C, La Rosa G, Daly TJ, Biochemistry. 1995 Sep 12;34(36):11399-409. PMID:7547867

Page seeded by OCA on Tue Jul 29 13:56:11 2008

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