1fzv

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(New page: 200px<br /> <applet load="1fzv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fzv, resolution 2.00&Aring;" /> '''THE CRYSTAL STRUCTU...)
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<applet load="1fzv" size="450" color="white" frame="true" align="right" spinBox="true"
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'''THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN AT 2.0A RESOLUTION'''<br />
'''THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN AT 2.0A RESOLUTION'''<br />
==Overview==
==Overview==
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The angiogenic molecule placenta growth factor (PlGF) is a member of the, cysteine-knot family of growth factors. In this study, a mature isoform of, the human PlGF protein, PlGF-1, was crystallized as a homodimer in the, crystallographic asymmetric unit, and its crystal structure was elucidated, at 2.0 A resolution. The overall structure of PlGF-1 is similar to that of, vascular endothelial growth factor (VEGF) with which it shares 42% amino, acid sequence identity. Based on structural and biochemical data, we have, mapped several important residues on the PlGF-1 molecule that are involved, in recognition of the fms-like tyrosine kinase receptor (Flt-1, also known, as VEGFR-1). We propose a model for the association of PlGF-1 and Flt-1, domain 2 with precise shape complementarity, consider the relevance of, this assembly for PlGF-1 signal transduction, and provide a structural, basis for altered specificity of this molecule.
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The angiogenic molecule placenta growth factor (PlGF) is a member of the cysteine-knot family of growth factors. In this study, a mature isoform of the human PlGF protein, PlGF-1, was crystallized as a homodimer in the crystallographic asymmetric unit, and its crystal structure was elucidated at 2.0 A resolution. The overall structure of PlGF-1 is similar to that of vascular endothelial growth factor (VEGF) with which it shares 42% amino acid sequence identity. Based on structural and biochemical data, we have mapped several important residues on the PlGF-1 molecule that are involved in recognition of the fms-like tyrosine kinase receptor (Flt-1, also known as VEGFR-1). We propose a model for the association of PlGF-1 and Flt-1 domain 2 with precise shape complementarity, consider the relevance of this assembly for PlGF-1 signal transduction, and provide a structural basis for altered specificity of this molecule.
==About this Structure==
==About this Structure==
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1FZV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FZV OCA].
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1FZV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FZV OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Acharya, K.R.]]
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[[Category: Acharya, K R.]]
[[Category: Battisti, M.]]
[[Category: Battisti, M.]]
[[Category: Iyer, S.]]
[[Category: Iyer, S.]]
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[[Category: Leonidas, D.D.]]
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[[Category: Leonidas, D D.]]
[[Category: Maglione, D.]]
[[Category: Maglione, D.]]
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[[Category: Persico, M.G.]]
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[[Category: Persico, M G.]]
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[[Category: Swaminathan, G.J.]]
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[[Category: Swaminathan, G J.]]
[[Category: Tucci, M.]]
[[Category: Tucci, M.]]
[[Category: MPD]]
[[Category: MPD]]
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[[Category: growth factor]]
[[Category: growth factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:58:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:25 2008''

Revision as of 10:44, 21 February 2008


1fzv, resolution 2.00Å

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THE CRYSTAL STRUCTURE OF HUMAN PLACENTA GROWTH FACTOR-1 (PLGF-1), AN ANGIOGENIC PROTEIN AT 2.0A RESOLUTION

Overview

The angiogenic molecule placenta growth factor (PlGF) is a member of the cysteine-knot family of growth factors. In this study, a mature isoform of the human PlGF protein, PlGF-1, was crystallized as a homodimer in the crystallographic asymmetric unit, and its crystal structure was elucidated at 2.0 A resolution. The overall structure of PlGF-1 is similar to that of vascular endothelial growth factor (VEGF) with which it shares 42% amino acid sequence identity. Based on structural and biochemical data, we have mapped several important residues on the PlGF-1 molecule that are involved in recognition of the fms-like tyrosine kinase receptor (Flt-1, also known as VEGFR-1). We propose a model for the association of PlGF-1 and Flt-1 domain 2 with precise shape complementarity, consider the relevance of this assembly for PlGF-1 signal transduction, and provide a structural basis for altered specificity of this molecule.

About this Structure

1FZV is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

The crystal structure of human placenta growth factor-1 (PlGF-1), an angiogenic protein, at 2.0 A resolution., Iyer S, Leonidas DD, Swaminathan GJ, Maglione D, Battisti M, Tucci M, Persico MG, Acharya KR, J Biol Chem. 2001 Apr 13;276(15):12153-61. Epub 2000 Nov 7. PMID:11069911

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