4hck: Difference between revisions
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[[Image:4hck.jpg|left|200px]] | [[Image:4hck.jpg|left|200px]] | ||
'''HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES''' | {{Structure | ||
|PDB= 4hck |SIZE=350|CAPTION= <scene name='initialview01'>4hck</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.7.112 2.1.7.112] | |||
|GENE= RESIDUES G72-E143 OF HUMAN HCK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
4HCK is a [ | 4HCK 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=4HCK OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of the human Hck SH3 domain and identification of its ligand binding site., Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA, J Mol Biol. 1998 Apr 24;278(1):253-65. PMID:[http:// | Solution structure of the human Hck SH3 domain and identification of its ligand binding site., Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA, J Mol Biol. 1998 Apr 24;278(1):253-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9571048 9571048] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''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 19:09:57 2008'' | ||
Revision as of 20:09, 20 March 2008
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| Gene: | RESIDUES G72-E143 OF HUMAN HCK (Homo sapiens) | ||||||
| Activity: | Transferase, with EC number 2.1.7.112 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES
OverviewOverview
SH3 domains are protein binding domains that occur widely among signal transduction proteins. Here, we present the NMR-determined solution structure of the SH3 domain from the cytoplasmic protein tyrosine kinase, Hck. Hck is involved in a number of cell signal transduction pathways, frequently in pathways associated with immune response. SH3 domains bind proteins via a left-handed polyproline type II helix on the target protein. We have assessed the structural impact of binding to a ligand through addition of a peptide corresponding to a proline-rich region of a Hck target, the GTPase activating protein of the Ras pathway. Ligand binding effects small structural changes and stabilizes the SH3 domain structure. Also, we have compared the solution structure of the Hck SH3 domain to the crystal structure of Hck, in which the SH3 domain exhibits an intramolecular binding to an interdomain linker region. These structures are interpreted as the apo- and holo- forms of the Hck SH3 domain.
About this StructureAbout this Structure
4HCK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of the human Hck SH3 domain and identification of its ligand binding site., Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA, J Mol Biol. 1998 Apr 24;278(1):253-65. PMID:9571048
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