Crystal structure of the Src family tyrosine kinase Hck - PubMed (original) (raw)
. 1997 Feb 13;385(6617):602-9.
doi: 10.1038/385602a0.
Affiliations
- PMID: 9024658
- DOI: 10.1038/385602a0
Crystal structure of the Src family tyrosine kinase Hck
F Sicheri et al. Nature. 1997.
Abstract
The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 A resolution. Inhibition of enzymatic activity is a consequence of intramolecular interactions of the enzyme's Src-homology domains SH2 and SH3, with concomitant displacement of elements of the catalytic domain. The conformation of the active site has similarities with that of inactive cyclin-dependent protein kinases.
Comment in
- New impressions of Src and Hck.
Pawson T. Pawson T. Nature. 1997 Feb 13;385(6617):582-3, 585. doi: 10.1038/385582b0. Nature. 1997. PMID: 9024653 No abstract available.
Similar articles
- Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement.
Moarefi I, LaFevre-Bernt M, Sicheri F, Huse M, Lee CH, Kuriyan J, Miller WT. Moarefi I, et al. Nature. 1997 Feb 13;385(6617):650-3. doi: 10.1038/385650a0. Nature. 1997. PMID: 9024665 - The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions.
Williams JC, Weijland A, Gonfloni S, Thompson A, Courtneidge SA, Superti-Furga G, Wierenga RK. Williams JC, et al. J Mol Biol. 1997 Dec 19;274(5):757-75. doi: 10.1006/jmbi.1997.1426. J Mol Biol. 1997. PMID: 9405157 - SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo.
Lerner EC, Smithgall TE. Lerner EC, et al. Nat Struct Biol. 2002 May;9(5):365-9. doi: 10.1038/nsb782. Nat Struct Biol. 2002. PMID: 11976726 - Structures of Src-family tyrosine kinases.
Sicheri F, Kuriyan J. Sicheri F, et al. Curr Opin Struct Biol. 1997 Dec;7(6):777-85. doi: 10.1016/s0959-440x(97)80146-7. Curr Opin Struct Biol. 1997. PMID: 9434895 Review. - Reading between the lines: SH3 recognition of an intact protein.
Lim WA. Lim WA. Structure. 1996 Jun 15;4(6):657-9. doi: 10.1016/s0969-2126(96)00071-8. Structure. 1996. PMID: 8805558 Review.
Cited by
- Cocrystallization of the Src-Family Kinase Hck with the ATP-Site Inhibitor A-419259 Stabilizes an Extended Activation Loop Conformation.
Selzer AM, Alvarado JJ, Smithgall TE. Selzer AM, et al. Biochemistry. 2024 Oct 15;63(20):2594-2601. doi: 10.1021/acs.biochem.4c00323. Epub 2024 Sep 24. Biochemistry. 2024. PMID: 39315638 Free PMC article. - A fluorescence-based sensor for calibrated measurement of protein kinase stability in live cells.
Paul JW 3rd, Muratcioğlu S, Kuriyan J. Paul JW 3rd, et al. Protein Sci. 2024 Jun;33(6):e5023. doi: 10.1002/pro.5023. Protein Sci. 2024. PMID: 38801214 Free PMC article. - A Fluorescence-Based Sensor for Calibrated Measurement of Protein Kinase Stability in Live Cells.
Paul JW 3rd, Muratcioğlu S, Kuriyan J. Paul JW 3rd, et al. bioRxiv [Preprint]. 2023 Dec 8:2023.12.07.570636. doi: 10.1101/2023.12.07.570636. bioRxiv. 2023. PMID: 38106090 Free PMC article. Updated. Preprint. - Src family kinases engage differential pathways for encapsulation into extracellular vesicles.
Ye C, Gosser C, Runyon ED, Zha J, Cai J, Beharry Z, Rickman CB, Klingeborn M, Liu Y, Xie J, Cai H. Ye C, et al. J Extracell Biol. 2023 Jun;2(6):e96. doi: 10.1002/jex2.96. Epub 2023 Jun 22. J Extracell Biol. 2023. PMID: 37588411 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous