1exz

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(New page: 200px<br /> <applet load="1exz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exz, resolution 2.3&Aring;" /> '''STRUCTURE OF STEM CE...)
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<applet load="1exz" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1exz, resolution 2.3&Aring;" />
'''STRUCTURE OF STEM CELL FACTOR'''<br />
'''STRUCTURE OF STEM CELL FACTOR'''<br />
==Overview==
==Overview==
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Stem cell factor (SCF) plays important roles in hematopoiesis and the, survival, proliferation, and differentiation of mast cells, melanocytes, and germ cells. SCF mediates its biological effects by binding to and, activating a receptor tyrosine kinase designated c-kit or SCF receptor. In, this report we describe the 2.3-A crystal structure of the functional core, of recombinant human SCF. SCF is a noncovalent homodimer composed of two, slightly wedged protomers. Each SCF protomer exhibits an antiparallel, four-helix bundle fold. Dimerization is mediated by extensive polar and, nonpolar interactions between the two protomers with a large buried, surface area. Finally, we have identified a hydrophobic crevice and a, charged region at the tail of each protomer that functions as a potential, receptor-binding site. On the basis of these observations, a model for SCF, small middle dotc-kit complex formation and dimerization is proposed.
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Stem cell factor (SCF) plays important roles in hematopoiesis and the survival, proliferation, and differentiation of mast cells, melanocytes, and germ cells. SCF mediates its biological effects by binding to and activating a receptor tyrosine kinase designated c-kit or SCF receptor. In this report we describe the 2.3-A crystal structure of the functional core of recombinant human SCF. SCF is a noncovalent homodimer composed of two slightly wedged protomers. Each SCF protomer exhibits an antiparallel four-helix bundle fold. Dimerization is mediated by extensive polar and nonpolar interactions between the two protomers with a large buried surface area. Finally, we have identified a hydrophobic crevice and a charged region at the tail of each protomer that functions as a potential receptor-binding site. On the basis of these observations, a model for SCF small middle dotc-kit complex formation and dimerization is proposed.
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==Disease==
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Known diseases associated with this structure: Skin/hair/eye pigmentation 7, blond/brown hair OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=184745 184745]]
==About this Structure==
==About this Structure==
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1EXZ 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 SM, CA and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXZ OCA].
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1EXZ 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=SM:'>SM</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXZ OCA].
==Reference==
==Reference==
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[[Category: scf]]
[[Category: scf]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:47:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:41 2008''

Revision as of 10:32, 21 February 2008

Image:1exz.gif

1exz, resolution 2.3Å

Drag the structure with the mouse to rotate

STRUCTURE OF STEM CELL FACTOR

Contents

Overview

Stem cell factor (SCF) plays important roles in hematopoiesis and the survival, proliferation, and differentiation of mast cells, melanocytes, and germ cells. SCF mediates its biological effects by binding to and activating a receptor tyrosine kinase designated c-kit or SCF receptor. In this report we describe the 2.3-A crystal structure of the functional core of recombinant human SCF. SCF is a noncovalent homodimer composed of two slightly wedged protomers. Each SCF protomer exhibits an antiparallel four-helix bundle fold. Dimerization is mediated by extensive polar and nonpolar interactions between the two protomers with a large buried surface area. Finally, we have identified a hydrophobic crevice and a charged region at the tail of each protomer that functions as a potential receptor-binding site. On the basis of these observations, a model for SCF small middle dotc-kit complex formation and dimerization is proposed.

Disease

Known diseases associated with this structure: Skin/hair/eye pigmentation 7, blond/brown hair OMIM:[184745]

About this Structure

1EXZ is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation., Zhang Z, Zhang R, Joachimiak A, Schlessinger J, Kong XP, Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7732-7. PMID:10884405

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