1ddm: Difference between revisions

Revision as of 13:15, 21 February 2008

SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE

OverviewOverview

The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb is involved in the formation of multiple protein complexes in vivo and can bind a diverse array of peptide sequences in vitro. To investigate the structural basis for the promiscuous nature of this protein module, we have determined its solution structure by NMR in a complex with a peptide containing an NMSF sequence derived from the Numb-associated kinase (Nak). The Nak peptide was found to adopt a significantly different structure from that of a GPpY sequence-containing peptide previously determined. In contrast to the helical turn adopted by the GPpY peptide, the Nak peptide forms a beta-turn at the NMSF site followed by another turn near the C-terminus. The Numb PTB domain appears to recognize peptides that differ in both primary and secondary structures by engaging various amounts of the binding surface of the protein. Our results suggest a mechanism through which a single PTB domain might interact with multiple distinct target proteins to control a complex biological process such as asymmetric cell division.

About this StructureAbout this Structure

1DDM is a Single protein structure of sequence from Drosophila melanogaster. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

Multiple modes of peptide recognition by the PTB domain of the cell fate determinant Numb., Zwahlen C, Li SC, Kay LE, Pawson T, Forman-Kay JD, EMBO J. 2000 Apr 3;19(7):1505-15. PMID:10747019

Page seeded by OCA on Thu Feb 21 12:15:32 2008

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OCA

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-[[Image:1ddm.gif|left|200px]]<br /><applet load="1ddm" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ddm.gif|left|200px]]<br /><applet load="1ddm" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ddm" />
 '''SOLUTION STRUCTURE OF THE NUMB PTB DOMAIN COMPLEXED TO A NAK PEPTIDE'''<br />
 ==Overview==
-The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb, is involved in the formation of multiple protein complexes in vivo and can, bind a diverse array of peptide sequences in vitro. To investigate the, structural basis for the promiscuous nature of this protein module, we, have determined its solution structure by NMR in a complex with a peptide, containing an NMSF sequence derived from the Numb-associated kinase (Nak)., The Nak peptide was found to adopt a significantly different structure, from that of a GPpY sequence-containing peptide previously determined. In, contrast to the helical turn adopted by the GPpY peptide, the Nak peptide, forms a beta-turn at the NMSF site followed by another turn near the, C-terminus. The Numb PTB domain appears to recognize peptides that differ, in both primary and secondary structures by engaging various amounts of, the binding surface of the protein. Our results suggest a mechanism, through which a single PTB domain might interact with multiple distinct, target proteins to control a complex biological process such as asymmetric, cell division.
+The phosphotyrosine-binding (PTB) domain of the cell fate determinant Numb is involved in the formation of multiple protein complexes in vivo and can bind a diverse array of peptide sequences in vitro. To investigate the structural basis for the promiscuous nature of this protein module, we have determined its solution structure by NMR in a complex with a peptide containing an NMSF sequence derived from the Numb-associated kinase (Nak). The Nak peptide was found to adopt a significantly different structure from that of a GPpY sequence-containing peptide previously determined. In contrast to the helical turn adopted by the GPpY peptide, the Nak peptide forms a beta-turn at the NMSF site followed by another turn near the C-terminus. The Numb PTB domain appears to recognize peptides that differ in both primary and secondary structures by engaging various amounts of the binding surface of the protein. Our results suggest a mechanism through which a single PTB domain might interact with multiple distinct target proteins to control a complex biological process such as asymmetric cell division.
 ==About this Structure==
-DDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DDM OCA].
+DDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DDM OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Non-specific serine/threonine protein kinase]]
 [[Category: Single protein]]
-[[Category: Forman-Kay, J.D.]]
+[[Category: Forman-Kay, J D.]]
-[[Category: Kay, L.E.]]
+[[Category: Kay, L E.]]
-[[Category: Li, S.C.]]
+[[Category: Li, S C.]]
 [[Category: Pawson, T.]]
 [[Category: Zwahlen, C.]]
@@ Line 24: / Line 24: @@
 [[Category: signal transduction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:11:47 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:32 2008''