2vkx
From Proteopedia
(New page: 200px<br /><applet load="2vkx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2vkx, resolution 2.7Å" /> '''HUMAN NCAM, FN3 DOMAI...) |
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| - | [[Image:2vkx.jpg|left|200px]] | + | [[Image:2vkx.jpg|left|200px]] |
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| - | '''HUMAN NCAM, FN3 DOMAINS 1 AND 2, M610R MUTANT''' | + | {{Structure |
| + | |PDB= 2vkx |SIZE=350|CAPTION= <scene name='initialview01'>2vkx</scene>, resolution 2.7Å | ||
| + | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+C'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+F'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Chain+F'>AC5</scene>, <scene name='pdbsite=AC6:So4+Binding+Site+For+Chain+A'>AC6</scene>, <scene name='pdbsite=AC7:So4+Binding+Site+For+Chain+F'>AC7</scene>, <scene name='pdbsite=AC8:So4+Binding+Site+For+Chain+E'>AC8</scene>, <scene name='pdbsite=AC9:So4+Binding+Site+For+Chain+D'>AC9</scene>, <scene name='pdbsite=BC1:So4+Binding+Site+For+Chain+F'>BC1</scene> and <scene name='pdbsite=BC2:So4+Binding+Site+For+Chain+F'>BC2</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN NCAM, FN3 DOMAINS 1 AND 2, M610R MUTANT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2VKX is a [ | + | 2VKX is a [[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=2VKX OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the Tandem Fibronectin Type 3 Domains of Neural Cell Adhesion Molecule., Carafoli F, Saffell JL, Hohenester E, J Mol Biol. 2008 Jan 17;. PMID:[http:// | + | Structure of the Tandem Fibronectin Type 3 Domains of Neural Cell Adhesion Molecule., Carafoli F, Saffell JL, Hohenester E, J Mol Biol. 2008 Jan 17;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18261743 18261743] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:47:31 2008'' |
Revision as of 16:47, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Sites: | , , , , , , , , , and | ||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN NCAM, FN3 DOMAINS 1 AND 2, M610R MUTANT
Overview
Activation of the fibroblast growth factor receptor (FGFR) by neural cell adhesion molecule (NCAM) is essential for NCAM-mediated neurite outgrowth. Previous peptide studies have identified two regions in the fibronectin type 3 (FN3)-like domains of NCAM as being important for these activities. Here we report the crystal structure of the NCAM FN3 domain tandem, which reveals an acutely bent domain arrangement. Mutation of a non-conserved surface residue (M610R) led to a second crystal form showing a substantially different conformation. Thus, the FN3 domain linker is highly flexible, suggesting that it corresponds to the hinge seen in electron micrographs of NCAM. The two putative FGFR1-binding segments, one in each NCAM FN3 domain, are situated close to the domain interface. They form a contiguous patch in the more severely bent conformation but become separated upon straightening of the FN3 tandem, suggesting that conformational changes within NCAM may modulate FGFR1 activation. Surface plasmon resonance experiments demonstrated only a very weak interaction between the NCAM FN3 tandem and soluble FGFR1 proteins expressed in mammalian cells (dissociation constant >100 muM). Thus, the NCAM-FGFR1 interaction at the cell surface is likely to depend upon avidity effects due to receptor clustering.
About this Structure
2VKX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the Tandem Fibronectin Type 3 Domains of Neural Cell Adhesion Molecule., Carafoli F, Saffell JL, Hohenester E, J Mol Biol. 2008 Jan 17;. PMID:18261743
Page seeded by OCA on Thu Mar 20 18:47:31 2008
