1olz
From Proteopedia
(New page: 200px<br /><applet load="1olz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1olz, resolution 2.00Å" /> '''THE LIGAND-BINDING F...) |
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| - | [[Image:1olz.jpg|left|200px]]<br /><applet load="1olz" size=" | + | [[Image:1olz.jpg|left|200px]]<br /><applet load="1olz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1olz, resolution 2.00Å" /> | caption="1olz, resolution 2.00Å" /> | ||
'''THE LIGAND-BINDING FACE OF THE SEMAPHORINS REVEALED BY THE HIGH RESOLUTION CRYSTAL STRUCTURE OF SEMA4D'''<br /> | '''THE LIGAND-BINDING FACE OF THE SEMAPHORINS REVEALED BY THE HIGH RESOLUTION CRYSTAL STRUCTURE OF SEMA4D'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal | + | Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1-657) shows the sema topology to be a seven-bladed beta-propeller, revealing an unexpected homology with integrins. The sema beta-propeller contains a distinctive 77-residue insertion between beta-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact cysteine knot abutting the side of the propeller, and an Ig-like domain. The top face of the beta-propeller presents prominent loops characteristic of semaphorins. In addition to limited contact between the Ig-like domains, the homodimer is stabilized through extensive interactions between the top faces in a sector of the beta-propeller used for heterodimerization in integrins. This face of the propeller also mediates ligand binding in integrins, and functional data for semaphorin-receptor interactions map to the equivalent surface. |
==About this Structure== | ==About this Structure== | ||
| - | 1OLZ 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:// | + | 1OLZ 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=1OLZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Davis, S | + | [[Category: Davis, S J.]] |
| - | [[Category: Esnouf, R | + | [[Category: Esnouf, R M.]] |
[[Category: Harlos, K.]] | [[Category: Harlos, K.]] | ||
| - | [[Category: Jones, E | + | [[Category: Jones, E Y.]] |
| - | [[Category: Love, C | + | [[Category: Love, C A.]] |
[[Category: Mavaddat, N.]] | [[Category: Mavaddat, N.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
| - | [[Category: Stuart, D | + | [[Category: Stuart, D I.]] |
[[Category: beta-propeller]] | [[Category: beta-propeller]] | ||
[[Category: cd100]] | [[Category: cd100]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:07 2008'' |
Revision as of 12:19, 21 February 2008
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THE LIGAND-BINDING FACE OF THE SEMAPHORINS REVEALED BY THE HIGH RESOLUTION CRYSTAL STRUCTURE OF SEMA4D
Overview
Semaphorins, proteins characterized by an extracellular sema domain, regulate axon guidance, immune function and angiogenesis. The crystal structure of SEMA4D (residues 1-657) shows the sema topology to be a seven-bladed beta-propeller, revealing an unexpected homology with integrins. The sema beta-propeller contains a distinctive 77-residue insertion between beta-strands C and D of blade 5. Blade 7 is followed by a domain common to plexins, semaphorins and integrins (PSI domain), which forms a compact cysteine knot abutting the side of the propeller, and an Ig-like domain. The top face of the beta-propeller presents prominent loops characteristic of semaphorins. In addition to limited contact between the Ig-like domains, the homodimer is stabilized through extensive interactions between the top faces in a sector of the beta-propeller used for heterodimerization in integrins. This face of the propeller also mediates ligand binding in integrins, and functional data for semaphorin-receptor interactions map to the equivalent surface.
About this Structure
1OLZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D., Love CA, Harlos K, Mavaddat N, Davis SJ, Stuart DI, Jones EY, Esnouf RM, Nat Struct Biol. 2003 Oct;10(10):843-8. Epub 2003 Sep 7. PMID:12958590
Page seeded by OCA on Thu Feb 21 14:19:07 2008
Categories: Homo sapiens | Single protein | Davis, S J. | Esnouf, R M. | Harlos, K. | Jones, E Y. | Love, C A. | Mavaddat, N. | SPINE, Structural Proteomics in Europe. | Stuart, D I. | Beta-propeller | Cd100 | Extracellular receptor | Glycoprotein developmental protein | Ig-like domain | Neurogenesis | Psi domain | Semaphorin | Spine | Structural genomics | Structural proteomics in europe
