Yes SH3 domainYes SH3 domain

Structural highlights

2hda is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:YES1, YES (Homo sapiens)
Activity:Non-specific protein-tyrosine kinase, with EC number 2.7.10.2
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

SH3 domains from the Src family of tyrosine kinases represent an interesting example of the delicate balance between promiscuity and specificity characteristic of proline-rich ligand recognition by SH3 domains. The development of inhibitors of therapeutic potential requires a good understanding of the molecular determinants of binding affinity and specificity and relies on the availability of high quality structural information. Here, we present the first high-resolution crystal structure of the SH3 domain of the c-Yes oncogen. Comparison with other SH3 domains from the Src family revealed significant deviations in the loop regions. In particular, the n-Src loop, highly flexible and partially disordered, is stabilized in an unusual conformation by the establishment of several intramolecular hydrogen bonds. Additionally, we present here the first report of amyloid aggregation by an SH3 domain from the Src family.

Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation.,Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Martin-Garcia JM, Luque I, Mateo PL, Ruiz-Sanz J, Camara-Artigas A. Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregation. FEBS Lett. 2007 May 1;581(9):1701-6. Epub 2007 Mar 30. PMID:17418139 doi:10.1016/j.febslet.2007.03.059

2hda, resolution 1.90Å

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