1u2h: Difference between revisions

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[[Image:1u2h.gif|left|200px]]<br />

[[Image:1u2h.gif|left|200px]]<br /><applet load="1u2h" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1u2h" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1u2h, resolution 0.96Å" />

'''X-ray Structure of the N-terminally truncated human APEP-1'''<br />

==Overview==

BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a, novel specific smooth muscle differentiation marker thought to play a role, in the growth and differentiation of arterial smooth muscle cells (SMCs)., RESULTS: Good quality crystals that were suitable for X-ray, crystallographic studies were obtained following the truncation of the 14, N-terminal amino acids of APEG-1, a region predicted to be disordered. The, truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin, (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition, motif. The RGD motif is crucial for the interaction of extracellular, proteins and plays a role in cell adhesion. The X-ray structure of, DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96, A). This is the best resolution for an immunoglobulin domain structure so, far. The structure adopts a Greek-key beta-sandwich fold and belongs to, the I (intermediate) set of the immunoglobulin superfamily. The residues, lying between the beta-sheets form a hydrophobic core. The RGD motif folds, into a 310 helix that is involved in the formation of a homodimer in the, crystal which is mainly stabilized by salt bridges. Analytical, ultracentrifugation studies revealed a moderate dissociation constant of, 20 microM at physiological ionic strength, suggesting that APEG-1, dimerisation is only transient in the cell. The binding constant is, strongly dependent on ionic strength. CONCLUSION: Our data suggests that, the RGD motif might play a role not only in the adhesion of extracellular, proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of, APEG-1 involving this motif is physiologically relevant.

BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant.

==About this Structure==

1U2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA].

1U2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA].

==Reference==

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[[Category: Gotz, F.]]

[[Category: Heinemann, U.]]

[[Category: Manjasetty, B.A.]]

[[Category: Manjasetty, B A.]]

[[Category: Niesen, F.H.]]

[[Category: Niesen, F H.]]

[[Category: Roske, Y.]]

[[Category: Scheich, C.]]

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[[Category: structural genomics]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1u2h.gif|left|200px]]<br />
+[[Image:1u2h.gif|left|200px]]<br /><applet load="1u2h" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1u2h" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1u2h, resolution 0.96&Aring;" />
 '''X-ray Structure of the N-terminally truncated human APEP-1'''<br />
 ==Overview==
-BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a, novel specific smooth muscle differentiation marker thought to play a role, in the growth and differentiation of arterial smooth muscle cells (SMCs)., RESULTS: Good quality crystals that were suitable for X-ray, crystallographic studies were obtained following the truncation of the 14, N-terminal amino acids of APEG-1, a region predicted to be disordered. The, truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin, (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition, motif. The RGD motif is crucial for the interaction of extracellular, proteins and plays a role in cell adhesion. The X-ray structure of, DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96, A). This is the best resolution for an immunoglobulin domain structure so, far. The structure adopts a Greek-key beta-sandwich fold and belongs to, the I (intermediate) set of the immunoglobulin superfamily. The residues, lying between the beta-sheets form a hydrophobic core. The RGD motif folds, into a 310 helix that is involved in the formation of a homodimer in the, crystal which is mainly stabilized by salt bridges. Analytical, ultracentrifugation studies revealed a moderate dissociation constant of, 20 microM at physiological ionic strength, suggesting that APEG-1, dimerisation is only transient in the cell. The binding constant is, strongly dependent on ionic strength. CONCLUSION: Our data suggests that, the RGD motif might play a role not only in the adhesion of extracellular, proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of, APEG-1 involving this motif is physiologically relevant.
+BACKGROUND: Human Aortic Preferentially Expressed Protein-1 (APEG-1) is a novel specific smooth muscle differentiation marker thought to play a role in the growth and differentiation of arterial smooth muscle cells (SMCs). RESULTS: Good quality crystals that were suitable for X-ray crystallographic studies were obtained following the truncation of the 14 N-terminal amino acids of APEG-1, a region predicted to be disordered. The truncated protein (termed DeltaAPEG-1) consists of a single immunoglobulin (Ig) like domain which includes an Arg-Gly-Asp (RGD) adhesion recognition motif. The RGD motif is crucial for the interaction of extracellular proteins and plays a role in cell adhesion. The X-ray structure of DeltaAPEG-1 was determined and was refined to sub-atomic resolution (0.96 A). This is the best resolution for an immunoglobulin domain structure so far. The structure adopts a Greek-key beta-sandwich fold and belongs to the I (intermediate) set of the immunoglobulin superfamily. The residues lying between the beta-sheets form a hydrophobic core. The RGD motif folds into a 310 helix that is involved in the formation of a homodimer in the crystal which is mainly stabilized by salt bridges. Analytical ultracentrifugation studies revealed a moderate dissociation constant of 20 microM at physiological ionic strength, suggesting that APEG-1 dimerisation is only transient in the cell. The binding constant is strongly dependent on ionic strength. CONCLUSION: Our data suggests that the RGD motif might play a role not only in the adhesion of extracellular proteins but also in intracellular protein-protein interactions. However, it remains to be established whether the rather weak dimerisation of APEG-1 involving this motif is physiologically relevant.
 ==About this Structure==
-U2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA].
+U2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U2H OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Gotz, F.]]
 [[Category: Heinemann, U.]]
-[[Category: Manjasetty, B.A.]]
+[[Category: Manjasetty, B A.]]
-[[Category: Niesen, F.H.]]
+[[Category: Niesen, F H.]]
 [[Category: Roske, Y.]]
 [[Category: Scheich, C.]]
@@ Line 28: / Line 27: @@
 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:30:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:55 2008''