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| - | [[Image:1nt3.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1nt3| PDB=1nt3 | SCENE= }} | | {{STRUCTURE_1nt3| PDB=1nt3 | SCENE= }} |
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| - | '''HUMAN NEUROTROPHIN-3'''
| + | ===HUMAN NEUROTROPHIN-3=== |
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| - | ==Overview==
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| - | Neurotrophin-3 (NT-3) is a cystine knot growth factor that promotes the survival, proliferation, and differentiation of developing neurons and is a potential therapeutic for neurodegenerative diseases. To clarify the structural basis of receptor specificity and the role of neurotrophin dimerization in receptor activation, the structure of the NT-3 homodimer was determined using X-ray crystallography. The orthorhombic crystals diffract to 2.4 A, with dimer symmetry occurring about a crystallographic 2-fold axis. The overall structure of NT-3 resembles that of the other neurotrophins, NGF and BDNF; each protomer forms a twisted four-stranded beta sheet, with three intertwined disulfide bonds. There are notable differences, however, between NT-3 and NGF in the surface loops and in three functionally important regions, shown in previous mutagenesis studies to be critical for binding. One such difference implies that NT-3's binding affinity and specificity depend on a novel hydrogen bond between Gln 83, a residue important for binding specificity with TrkC, and Arg 103, a residue crucial for binding affinity with TrkC. NT-3's extensive dimer interface buries much of the otherwise solvent-accessible hydrophobic surface area and suggests that the dimeric state is stabilized through the formation of this hydrophobic core. A comparison of the dimer interface between the NT-3 homodimer and the BDNF/NT-3 heterodimer reveals similar patterns of hydrogen bonds and nonpolar contacts, which reinforces the notion that the evolutionarily conserved neurotrophin interface resulted from the need for receptor dimerization in signal initiation.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9836577}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9836577 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9836577}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Growth factor]] | | [[Category: Growth factor]] |
| | [[Category: Neurotrophin]] | | [[Category: Neurotrophin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:56:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:34:51 2008'' |
Revision as of 00:34, 28 July 2008
Template:STRUCTURE 1nt3
HUMAN NEUROTROPHIN-3
Template:ABSTRACT PUBMED 9836577
About this Structure
1NT3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of neurotrophin-3 homodimer shows distinct regions are used to bind its receptors., Butte MJ, Hwang PK, Mobley WC, Fletterick RJ, Biochemistry. 1998 Dec 1;37(48):16846-52. PMID:9836577
Page seeded by OCA on Mon Jul 28 03:34:51 2008
