1uj0
From Proteopedia
(New page: 200px<br /><applet load="1uj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uj0, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:1uj0.jpg|left|200px]]<br /><applet load="1uj0" size=" | + | [[Image:1uj0.jpg|left|200px]]<br /><applet load="1uj0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uj0, resolution 1.70Å" /> | caption="1uj0, resolution 1.70Å" /> | ||
'''Crystal Structure of STAM2 SH3 domain in complex with a UBPY-derived peptide'''<br /> | '''Crystal Structure of STAM2 SH3 domain in complex with a UBPY-derived peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Although some exceptional motifs have been identified, it is well known | + | Although some exceptional motifs have been identified, it is well known that the PXXP motif is the motif of ligand proteins generally recognized by the Src homology 3 (SH3) domain. SH3-ligand interactions are usually weak, with ordinary KD approximately 10 microM. The structural basis for a tight and specific association (KD = 0.24 microm) between Gads SH3 and a novel motif, PX(V/I)(D/N)RXXKP, was revealed in a previous structural analysis of the complex formed between them. In this paper, we report the crystal structure of the signal transducing adaptor molecule-2 (STAM2) SH3 domain in complex with a peptide with a novel motif derived from a ligand protein, UBPY. The derived KD value for this complex is 27 microM. The notable difference in affinity for these parallel complexes may be explained because the STAM2 SH3 structure does not provide a specificity pocket for binding, whereas the Gads SH3 structure does. Instead, the structure of STAM2 SH3 is analogous to that of Grb2 SH3 which, in addition to normal PXXP ligands, has also been shown to moderately recognize the novel motif discussed herein. Thus, the extremely tight interaction observed between Gads SH3 and the novel motif is caused not by an innate ability of the novel motif but rather by an evolutionary change in the Gads SH3 domain. Instead, SH3 domains of STAM2 and Grb2 retain the moderate characteristics of recognizing their ligand proteins like other SH3 domains for appropriate transient interactions between signaling molecules. |
==About this Structure== | ==About this Structure== | ||
| - | 1UJ0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1UJ0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJ0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: stam]] | [[Category: stam]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:02 2008'' |
Revision as of 13:25, 21 February 2008
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Crystal Structure of STAM2 SH3 domain in complex with a UBPY-derived peptide
Overview
Although some exceptional motifs have been identified, it is well known that the PXXP motif is the motif of ligand proteins generally recognized by the Src homology 3 (SH3) domain. SH3-ligand interactions are usually weak, with ordinary KD approximately 10 microM. The structural basis for a tight and specific association (KD = 0.24 microm) between Gads SH3 and a novel motif, PX(V/I)(D/N)RXXKP, was revealed in a previous structural analysis of the complex formed between them. In this paper, we report the crystal structure of the signal transducing adaptor molecule-2 (STAM2) SH3 domain in complex with a peptide with a novel motif derived from a ligand protein, UBPY. The derived KD value for this complex is 27 microM. The notable difference in affinity for these parallel complexes may be explained because the STAM2 SH3 structure does not provide a specificity pocket for binding, whereas the Gads SH3 structure does. Instead, the structure of STAM2 SH3 is analogous to that of Grb2 SH3 which, in addition to normal PXXP ligands, has also been shown to moderately recognize the novel motif discussed herein. Thus, the extremely tight interaction observed between Gads SH3 and the novel motif is caused not by an innate ability of the novel motif but rather by an evolutionary change in the Gads SH3 domain. Instead, SH3 domains of STAM2 and Grb2 retain the moderate characteristics of recognizing their ligand proteins like other SH3 domains for appropriate transient interactions between signaling molecules.
About this Structure
1UJ0 is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain., Kaneko T, Kumasaka T, Ganbe T, Sato T, Miyazawa K, Kitamura N, Tanaka N, J Biol Chem. 2003 Nov 28;278(48):48162-8. Epub 2003 Sep 16. PMID:13129930
Page seeded by OCA on Thu Feb 21 15:25:02 2008
Categories: Mus musculus | Protein complex | Ganbe, T. | Kaneko, T. | Kitamura, N. | Kumasaka, T. | Miyazawa, K. | Sato, T. | Tanaka, N. | PO4 | Deubiquitinating enzyme | Early endosome | Endocytosis | Gads | Grb2 | Hrs | Pxxp | Sh3 | Stam
