1qwf
From Proteopedia
(New page: 200px<br /><applet load="1qwf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwf" /> '''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12...) |
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| - | [[Image:1qwf.jpg|left|200px]]<br /><applet load="1qwf" size=" | + | [[Image:1qwf.jpg|left|200px]]<br /><applet load="1qwf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qwf" /> | caption="1qwf" /> | ||
'''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12'''<br /> | '''C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) | + | Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1QWF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. 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:// | + | 1QWF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus]. 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=1QWF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chiyoshi, K.]] | [[Category: Chiyoshi, K.]] | ||
[[Category: Feng, S.]] | [[Category: Feng, S.]] | ||
| - | [[Category: Rickles, R | + | [[Category: Rickles, R J.]] |
| - | [[Category: Schreiber, S | + | [[Category: Schreiber, S L.]] |
[[Category: class i ligand complex]] | [[Category: class i ligand complex]] | ||
[[Category: src sh3 domain]] | [[Category: src sh3 domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:24 2008'' |
Revision as of 12:44, 21 February 2008
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C-SRC SH3 DOMAIN COMPLEXED WITH LIGAND VSL12
Overview
Two dodecapeptides belonging to distinct classes of Src homology 3 (SH3) ligands and selected from biased phage display libraries were used to investigate interactions between a specificity pocket in the Src SH3 domain and ligant residues flanking the proline-rich core. The solution structures of c-Src SH3 complexed with these peptides were solved by NMR. In addition to proline-rich, polyproline type II helix-forming core, the class I and II ligands each possesses a flanking sequence that occupies a large pocket between the RT and n-Src loops of the SH3 domain. Structural and mutational analyses illustrate how the two classes of SH3 ligands exploit a specificity pocket on the receptor differently to increase binding affinity and specificity.
About this Structure
1QWF is a Single protein structure of sequence from Avian sarcoma virus. 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
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands., Feng S, Kasahara C, Rickles RJ, Schreiber SL, Proc Natl Acad Sci U S A. 1995 Dec 19;92(26):12408-15. PMID:8618911
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