1hmc

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(New page: 200px<br /> <applet load="1hmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmc, resolution 2.5&Aring;" /> '''THREE-DIMENSIONAL ST...)
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'''THREE-DIMENSIONAL STRUCTURE OF DIMERIC HUMAN RECOMBINANT MACROPHAGE COLONY STIMULATING FACTOR'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF DIMERIC HUMAN RECOMBINANT MACROPHAGE COLONY STIMULATING FACTOR'''<br />
==Overview==
==Overview==
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Macrophage colony-stimulating factor (M-CSF) triggers the development of, cells of the monocyte-macrophage lineage and has a variety of stimulatory, effects on mature cells of this class. The biologically active form of, M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine, kinase activity on the M-CSF receptor by inducing dimerization of the, receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles, of four alpha helices laid end-to-end, with an interchain disulfide bond., Individual monomers of M-CSF show a close structural similarity to the, cytokines granulocyte-macrophage colony-stimulating factor and human, growth hormone. Both of these cytokines are monomeric in their active, form, and their specific receptors lack intrinsic tyrosine kinase, activity. The similarity of these structures suggests that the receptor, binding determinants for all three cytokines may be similar.
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Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1HMC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HMC OCA].
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1HMC is a [http://en.wikipedia.org/wiki/Single_protein 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=1HMC OCA].
==Reference==
==Reference==
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[[Category: Halenbeck, R.]]
[[Category: Halenbeck, R.]]
[[Category: Jancarik, J.]]
[[Category: Jancarik, J.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
[[Category: Koths, K.]]
[[Category: Koths, K.]]
[[Category: Pandit, J.]]
[[Category: Pandit, J.]]
[[Category: macrophage colony stimulating factor]]
[[Category: macrophage colony stimulating factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:20:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:52 2008''

Revision as of 11:02, 21 February 2008


1hmc, resolution 2.5Å

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THREE-DIMENSIONAL STRUCTURE OF DIMERIC HUMAN RECOMBINANT MACROPHAGE COLONY STIMULATING FACTOR

Contents

Overview

Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.

Disease

Known disease associated with this structure: Myeloid malignancy, predisposition to OMIM:[164770]

About this Structure

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

Reference

Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor., Pandit J, Bohm A, Jancarik J, Halenbeck R, Koths K, Kim SH, Science. 1992 Nov 20;258(5086):1358-62. PMID:1455231

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