1abq: Difference between revisions
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[[Image:1abq.jpg|left|200px]] | [[Image:1abq.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN''' | {{Structure | ||
|PDB= 1abq |SIZE=350|CAPTION= <scene name='initialview01'>1abq</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ABQ is a [ | 1ABQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ABQ OCA]. | ||
==Reference== | ==Reference== | ||
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides., Musacchio A, Saraste M, Wilmanns M, Nat Struct Biol. 1994 Aug;1(8):546-51. PMID:[http:// | High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides., Musacchio A, Saraste M, Wilmanns M, Nat Struct Biol. 1994 Aug;1(8):546-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7664083 7664083] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase (phosphotransferase)]] | [[Category: transferase (phosphotransferase)]] | ||
''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 09:55:28 2008'' | ||
Revision as of 07:55, 20 March 2008
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| 1abq, resolution 2.8Å | |||||||||||||
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| Activity: | Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN
Overview
Src-homology 3 (SH3) domains bind to proline-rich motifs in target proteins. We have determined high-resolution crystal structures of the complexes between the SH3 domains of Abl and Fyn tyrosine kinases, and two ten-residue proline-rich peptides derived from the SH3-binding proteins 3BP-1 and 3BP-2. The X-ray data show that the basic mode of binding of both proline-rich peptides is the same. Peptides are bound over their entire length and interact with three major sites on the SH3 molecules by both hydrogen-bonding and van der Waals contacts. Residues 4-10 of the peptide adopt the conformation of a left-handed polyproline helix type II. Binding of the proline at position 2 requires a kink at the non-proline position 3.
About this Structure
1ABQ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides., Musacchio A, Saraste M, Wilmanns M, Nat Struct Biol. 1994 Aug;1(8):546-51. PMID:7664083
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