1fyn
From Proteopedia
(New page: 200px<br /> <applet load="1fyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fyn, resolution 2.30Å" /> '''PHOSPHOTRANSFERASE'...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1fyn.gif|left|200px]]<br /> | + | [[Image:1fyn.gif|left|200px]]<br /><applet load="1fyn" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1fyn" size=" | + | |
caption="1fyn, resolution 2.30Å" /> | caption="1fyn, resolution 2.30Å" /> | ||
'''PHOSPHOTRANSFERASE'''<br /> | '''PHOSPHOTRANSFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Src-homology 3 (SH3) domains bind to proline-rich motifs in target | + | 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== | ==About this Structure== | ||
| - | 1FYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | + | 1FYN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYN OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 26: | ||
[[Category: tyrosine-protein kinase]] | [[Category: tyrosine-protein kinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:05 2008'' |
Revision as of 10:44, 21 February 2008
|
PHOSPHOTRANSFERASE
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
1FYN is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 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
Page seeded by OCA on Thu Feb 21 12:44:05 2008
