Access the full text.
Sign up today, get DeepDyve free for 14 days.
G. Waksman, S. Shoelson, N. Pant, D. Cowburn, J. Kuriyan (1993)
Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 72
H. Piwnica-Worms, K. Saunders, T. Roberts, Alan Smith, Seng Cheng (1987)
Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-srcCell, 49
TE Kmiecik, D Shalloway (1987)
Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylationCell, 49
J. Pines (1995)
Confirmational changeNature, 376
S. Ziegler, J. Marth, D. Lewis, R. Perlmutter (1987)
Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic originMolecular and Cellular Biology, 7
A. Adzhubei, M. Sternberg (1993)
Left-handed polyproline II helices commonly occur in globular proteins.Journal of molecular biology, 229 2
T. Jones, J. Zou, S. Cowan, M. Kjeldgaard, Serge HAGgGE (1991)
Improved methods for building protein models in electron density maps and the location of errors in these models.Acta crystallographica. Section A, Foundations of crystallography, 47 ( Pt 2)
C. Cartwright, W. Eckhart, S. Simon, P. Kaplan (1987)
Cell transformation by pp60c-src mutated in the carboxy-terminal regulatory domainCell, 49
J. Ladbury, M. Lemmon, Min Zhou, Jeremy Green, M. Botfield, J. Schlessinger (1995)
Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal.Proceedings of the National Academy of Sciences of the United States of America, 92
M. Eck, S. Atwell, S. Shoelson, S. Harrison (1994)
Structure of the regulatory domains of the Src-family tyrosine kinase LckNature, 368
T. Pawson (1995)
Protein modules and signalling networksNature, 373
M. Eck, S. Shoelson, S. Harrison (1993)
Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lckNature, 362
A. Brunger (1988)
Crystallographic refinement by simulated annealingJournal of Molecular Biology, 203
J. Cooper, C. King (1986)
Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-srcMolecular and Cellular Biology, 6
S. Hubbard, Lei Wei, W. Hendrickson (1994)
Crystal structure of the tyrosine kinase domain of the human insulin receptorNature, 372
M. Carson (1991)
RIBBONS 2.0Journal of Applied Crystallography, 24
G. Cohen, R. Ren, D. Baltimore (1995)
Modular binding domains in signal transduction proteinsCell, 80
D. Knighton, Jianhua Zheng, L. Eyck, V. Ashford, N. Xuong, S. Taylor, J. Sowadski (1991)
Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.Science, 253 5018
Chi-Hon Lee, K. Saksela, U. Mirza, B. Chait, J. Kuriyan (1996)
Crystal Structure of the Conserved Core of HIV-1 Nef Complexed with a Src Family SH3 DomainCell, 85
G. Waksman, D. Kominos, S. Robertson, N. Pant, D. Baltimore, R. Birge, D. Cowburn, H. Hanafusa, B. Mayer, M. Overduin, M. Resh, C. Ríos, L. Silverman, J. Kuriyan (1993)
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptidesNature, 358
MJ Eck, SK Atwell, SE Shoelson, SC Harrison (1994)
Crystal structure of the regulatory domains of the Src-family tyrosine kinase lckNature, 368
AR Brünger (1992)
X-PLOR
Chi-Hon Lee, Benjamin Leung, M. Lemmon, Jie Zheng, D. Cowburn, J. Kuriyan, K. Saksela (1995)
A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV‐1 Nef protein.The EMBO Journal, 14
P. Jeffrey, A. Russo, K. Polyak, E. Gibbs, J. Hurwitz, J. Massagué, N. Pavletich (1995)
Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complexNature, 376
Songyang Zhou, S. Shoelson, M. Chaudhuri, G. Gish, T. Pawson, W. Haser, Fred King, T. Roberts, S. Ratnofsky, R. Lechleider, B. Neel, R. Birge, J. Fajardo, M. Chou, H. Hanafusa, B. Schaffhausen, L. Cantley (1993)
SH2 domains recognize specific phosphopeptide sequencesCell, 72
N. Quintrell, R. Lebo, H. Varmus, J. Bishop, M. Pettenati, M. Beau, Manuel Diaz, Janet Rowley (1987)
Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cellsMolecular and Cellular Biology, 7
L. Johnson, M. Noble, D. Owen (1996)
Active and Inactive Protein Kinases: Structural Basis for RegulationCell, 85
H. Bondt, J. Rosenblatt, J. Jancarik, H. Jones, David Morgant, Sung-Hou Kim (1993)
Crystal structure of cyclin-dependent kinase 2Nature, 363
TJ Parsons, MJ Weber (1989)
Genetics of src. structure and functal organization of a protein tyrosine kinaseCurr. Top. Microb. Immunol., 147
B. Cunningham, M. Threadgill, P. Groundwater, I. Dale, J. Hickman (1992)
Synthesis and biological evaluation of a series of flavones designed as inhibitors of protein tyrosine kinases.Anti-cancer drug design, 7 5
K. Alexandropoulos, D. Baltimore (1996)
Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel p130Cas-related protein, Sin.Genes & development, 10 11
W. Lim, F. Richards, R. Fox (1995)
Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domainsNature, 372
C. Lowell, M. Niwa, Philippe Soriano, H. Varmus (1996)
Deficiency of the Hck and Src tyrosine kinases results in extreme levels of extramedullary hematopoiesis.Blood, 87 5
I. Moarefi, M. LaFevre-Bernt, F. Sicheri, M. Huse, Chi-Hon Lee, J. Kuriyan, W. Miller (1997)
Activation of the Sire-family tyrosine kinase Hck by SH3 domain displacementNature, 385
S. Briggs, S. Bryant, R. Jove, S. Sanderson, T. Smithgall (1995)
The Ras GTPase-activating Protein (GAP) Is an SH3 Domain-binding Protein and Substrate for the Src-related Tyrosine Kinase, Hck (*)The Journal of Biological Chemistry, 270
Hongtao Yu, James Chen, S. Feng, D. Dalgarno, A. Brauer, Stuart Schrelber (1994)
Structural basis for the binding of proline-rich peptides to SH3 domainsCell, 76
W Furey, S Swaminathan (1990)
American Crystallographic Association Meeting Abstracts
A. Nicholls, K. Sharp, B. Honig (1991)
Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbonsProteins: Structure, 11
A. Musacchio, M. Saraste, M. Wilmanns (1994)
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptidesNature Structural Biology, 1
A. Macauley, J. Cooper (1989)
Structural differences between repressed and derepressed forms of p60c-srcMolecular and Cellular Biology, 9
S. Courtneidge (1985)
Activation of the pp60c‐src kinase by middle T antigen binding or by dephosphorylation.The EMBO Journal, 4
Jian-Xin Zheng, E. Trafny, D. Knighton, N. Xuong, Susan Taylor, L. Eyck, J. Sowadski (1993)
2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor.Acta crystallographica. Section D, Biological crystallography, 49 Pt 3
H. Yamaguchi, W. Hendrickson (1996)
Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylationNature, 384
AT Brünger (1988)
Crystallographic refinement by simulated annealing: application to a 2.8 Å resolution structure of aspartate aminotransferaseJ. Mol. Biol., 203
C. Lowell, Philippe Soriano, H. Varmus (1994)
Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity.Genes & development, 8 4
CA Cartwright, W Eckhart, S Simon, PL Kaplan (1987)
Cell transformation by pp60c-Src mutated in the carboxy-terminal regulatory domainCell, 49
M. Brown, Jonathan Cooper (1996)
Regulation, substrates and functions of src.Biochimica et biophysica acta, 1287 2-3
T. Kmiecik, D. Shalloway (1987)
Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylationCell, 49
T. Erpel, G. Superti-Furga, Sara Courtneidgel (1995)
Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra‐ and intermolecular interactions.The EMBO Journal, 14
A. Musacchio, M. Noble, R. Pauptit, R. Wierenga, M. Saraste (1992)
Crystal structure of a Src-homology 3 (SH3) domainNature, 359
The crystal structure of the haematopoietic cell kinase Hck has been determined at 2.6/2.9 Å 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.
Nature – Springer Journals
Published: Feb 13, 1997
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.