1shg
From Proteopedia
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| - | [[Image:1shg.jpg|left|200px]] | + | [[Image:1shg.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN''' | + | {{Structure |
| + | |PDB= 1shg |SIZE=350|CAPTION= <scene name='initialview01'>1shg</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SHG is a [ | + | 1SHG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHG OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a Src-homology 3 (SH3) domain., Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M, Nature. 1992 Oct 29;359(6398):851-5. PMID:[http:// | + | Crystal structure of a Src-homology 3 (SH3) domain., Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M, Nature. 1992 Oct 29;359(6398):851-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1279434 1279434] |
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cytoskeleton]] | [[Category: cytoskeleton]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:04:57 2008'' |
Revision as of 12:05, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN
Overview
The Src-homologous SH3 domain is a small domain present in a large number of proteins that are involved in signal transduction, such as the Src protein tyrosine kinase, or in membrane-cytoskeleton interactions, but the function of SH3 is still unknown (reviewed in refs 1-3). Here we report the three-dimensional structure at 1.8 A resolution of the SH3 domain of the cytoskeletal protein spectrin expressed in Escherichia coli. The domain is a compact beta-barrel made of five antiparallel beta-strands. The amino acids that are conserved in the SH3 sequences are located close to each other on one side of the molecule. This surface is rich in aromatic and carboxylic amino acids, and is distal to the region of the molecule where the N and C termini reside and where SH3 inserts into the alpha-spectrin chain. We suggest that a protein ligand binds to this conserved surface of SH3.
About this Structure
1SHG is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a Src-homology 3 (SH3) domain., Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M, Nature. 1992 Oct 29;359(6398):851-5. PMID:1279434
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