1exz

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|PDB= 1exz |SIZE=350|CAPTION= <scene name='initialview01'>1exz</scene>, resolution 2.3&Aring;
|PDB= 1exz |SIZE=350|CAPTION= <scene name='initialview01'>1exz</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1exz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exz OCA], [http://www.ebi.ac.uk/pdbsum/1exz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1exz RCSB]</span>
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}}
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==Overview==
==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.
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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[[Category: Zhang, R.]]
[[Category: Zhang, R.]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z.]]
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[[Category: CA]]
 
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[[Category: SM]]
 
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[[Category: TRS]]
 
[[Category: scf]]
[[Category: scf]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:50 2008''

Revision as of 17:11, 30 March 2008


PDB ID 1exz

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF STEM CELL FACTOR


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.

About this Structure

1EXZ is a Single protein structure of sequence from Homo sapiens. 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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