1n81

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(New page: 200px<br /><applet load="1n81" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n81, resolution 2.10&Aring;" /> '''Crystal structure of...)
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caption="1n81, resolution 2.10&Aring;" />
'''Crystal structure of Pfg27 from Plasmodium falciparum'''<br />
'''Crystal structure of Pfg27 from Plasmodium falciparum'''<br />
==Overview==
==Overview==
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Malaria transmission is dependent on the development of sexual forms of, Plasmodium falciparum, called gametocytes, in the vertebrate host. Pfg27, is an abundantly expressed sexual stage-specific protein that is essential, for gametocytogenesis in P. falciparum. We describe the crystal structure, of Pfg27, which reveals a novel fold composed of two pseudo dyad-related, repeats of the helix-turn-helix motif. Structurally equivalent helices of, each repeat either form a dimer interface or interact with RNA in vitro., One side of the dimer presents an unprecedented juxtaposition of four, polyproline (PXXP) motifs. Preliminary binding data indicate that these, sites are capable of binding Src homology-3 (SH3) modules. Molecular, modeling suggests that the dimer can accommodate two SH3 modules, simultaneously, potentially enabling molecular crosstalk between, SH3-containing proteins. The structural and initial biochemical evidence, suggests that Pfg27 may serve as a platform for RNA and SH3 binding.
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Malaria transmission is dependent on the development of sexual forms of Plasmodium falciparum, called gametocytes, in the vertebrate host. Pfg27 is an abundantly expressed sexual stage-specific protein that is essential for gametocytogenesis in P. falciparum. We describe the crystal structure of Pfg27, which reveals a novel fold composed of two pseudo dyad-related repeats of the helix-turn-helix motif. Structurally equivalent helices of each repeat either form a dimer interface or interact with RNA in vitro. One side of the dimer presents an unprecedented juxtaposition of four polyproline (PXXP) motifs. Preliminary binding data indicate that these sites are capable of binding Src homology-3 (SH3) modules. Molecular modeling suggests that the dimer can accommodate two SH3 modules simultaneously, potentially enabling molecular crosstalk between SH3-containing proteins. The structural and initial biochemical evidence suggests that Pfg27 may serve as a platform for RNA and SH3 binding.
==About this Structure==
==About this Structure==
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1N81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N81 OCA].
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1N81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N81 OCA].
==Reference==
==Reference==
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[[Category: pxxp]]
[[Category: pxxp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:42:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:14 2008''

Revision as of 12:03, 21 February 2008


1n81, resolution 2.10Å

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Crystal structure of Pfg27 from Plasmodium falciparum

Overview

Malaria transmission is dependent on the development of sexual forms of Plasmodium falciparum, called gametocytes, in the vertebrate host. Pfg27 is an abundantly expressed sexual stage-specific protein that is essential for gametocytogenesis in P. falciparum. We describe the crystal structure of Pfg27, which reveals a novel fold composed of two pseudo dyad-related repeats of the helix-turn-helix motif. Structurally equivalent helices of each repeat either form a dimer interface or interact with RNA in vitro. One side of the dimer presents an unprecedented juxtaposition of four polyproline (PXXP) motifs. Preliminary binding data indicate that these sites are capable of binding Src homology-3 (SH3) modules. Molecular modeling suggests that the dimer can accommodate two SH3 modules simultaneously, potentially enabling molecular crosstalk between SH3-containing proteins. The structural and initial biochemical evidence suggests that Pfg27 may serve as a platform for RNA and SH3 binding.

About this Structure

1N81 is a Single protein structure of sequence from Plasmodium falciparum 3d7. Full crystallographic information is available from OCA.

Reference

Structure of a gametocyte protein essential for sexual development in Plasmodium falciparum., Sharma A, Sharma I, Kogkasuriyachai D, Kumar N, Nat Struct Biol. 2003 Mar;10(3):197-203. PMID:12577051

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