2c8i: Difference between revisions

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[[Image:2c8i.gif|left|200px]]<br />

[[Image:2c8i.gif|left|200px]]<br /><applet load="2c8i" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2c8i" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2c8i" />

'''COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 1, 2, 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A'''<br />

==Overview==

Many enteroviruses bind to the complement control protein, decay-accelerating factor (DAF) to facilitate cell entry. We present here, a structure for echovirus (EV) type 12 bound to DAF using cryo-negative, stain transmission electron microscopy and three-dimensional image, reconstruction to 16-A resolution, which we interpreted using the atomic, structures of EV11 and DAF. DAF binds to a hypervariable region of the, capsid close to the 2-fold symmetry axes in an interaction that involves, mostly the short consensus repeat 3 domain of DAF and the capsid protein, VP2. A bulge in the density for the short consensus repeat 3 domain, suggests that a loop at residues 174-180 rearranges to prevent steric, collision between closely packed molecules at the 2-fold symmetry axes., Detailed analysis of receptor interactions between a variety of, echoviruses and DAF using surface plasmon resonance and comparison of this, structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J., Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound, to DAF support major differences in receptor recognition among these, viruses. However, comparison of the electron density for the two, virus.receptor complexes (rather than comparisons of the pseudo-atomic, models derived from fitting the coordinates into these densities) suggests, that the dramatic differences in interaction affinities/specificities may, arise from relatively subtle structural differences rather than from, large-scale repositioning of the receptor with respect to the virus, surface.

Many enteroviruses bind to the complement control protein decay-accelerating factor (DAF) to facilitate cell entry. We present here a structure for echovirus (EV) type 12 bound to DAF using cryo-negative stain transmission electron microscopy and three-dimensional image reconstruction to 16-A resolution, which we interpreted using the atomic structures of EV11 and DAF. DAF binds to a hypervariable region of the capsid close to the 2-fold symmetry axes in an interaction that involves mostly the short consensus repeat 3 domain of DAF and the capsid protein VP2. A bulge in the density for the short consensus repeat 3 domain suggests that a loop at residues 174-180 rearranges to prevent steric collision between closely packed molecules at the 2-fold symmetry axes. Detailed analysis of receptor interactions between a variety of echoviruses and DAF using surface plasmon resonance and comparison of this structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J. Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound to DAF support major differences in receptor recognition among these viruses. However, comparison of the electron density for the two virus.receptor complexes (rather than comparisons of the pseudo-atomic models derived from fitting the coordinates into these densities) suggests that the dramatic differences in interaction affinities/specificities may arise from relatively subtle structural differences rather than from large-scale repositioning of the receptor with respect to the virus surface.

==Disease==

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==About this Structure==

2C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA].

2C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA].

==Reference==

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[[Category: Protein complex]]

[[Category: Bhella, D.]]

[[Category: Evans, D.J.]]

[[Category: Evans, D J.]]

[[Category: Kerrigan, D.]]

[[Category: Lea, S.M.]]

[[Category: Lea, S M.]]

[[Category: Pettigrew, D.M.]]

[[Category: Pettigrew, D M.]]

[[Category: Williams, D.T.]]

[[Category: Williams, D T.]]

[[Category: antigen]]

[[Category: blood group antigen]]

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[[Category: virus-receptor complex]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12~~ 21:12:~~32 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:06 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2c8i.gif|left|200px]]<br />
+[[Image:2c8i.gif|left|200px]]<br /><applet load="2c8i" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2c8i" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2c8i" />
 '''COMPLEX OF ECHOVIRUS TYPE 12 WITH DOMAINS 1, 2, 3 AND 4 OF ITS RECEPTOR DECAY ACCELERATING FACTOR (CD55) BY CRYO ELECTRON MICROSCOPY AT 16 A'''<br />
 ==Overview==
-Many enteroviruses bind to the complement control protein, decay-accelerating factor (DAF) to facilitate cell entry. We present here, a structure for echovirus (EV) type 12 bound to DAF using cryo-negative, stain transmission electron microscopy and three-dimensional image, reconstruction to 16-A resolution, which we interpreted using the atomic, structures of EV11 and DAF. DAF binds to a hypervariable region of the, capsid close to the 2-fold symmetry axes in an interaction that involves, mostly the short consensus repeat 3 domain of DAF and the capsid protein, VP2. A bulge in the density for the short consensus repeat 3 domain, suggests that a loop at residues 174-180 rearranges to prevent steric, collision between closely packed molecules at the 2-fold symmetry axes., Detailed analysis of receptor interactions between a variety of, echoviruses and DAF using surface plasmon resonance and comparison of this, structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J., Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound, to DAF support major differences in receptor recognition among these, viruses. However, comparison of the electron density for the two, virus.receptor complexes (rather than comparisons of the pseudo-atomic, models derived from fitting the coordinates into these densities) suggests, that the dramatic differences in interaction affinities/specificities may, arise from relatively subtle structural differences rather than from, large-scale repositioning of the receptor with respect to the virus, surface.
+Many enteroviruses bind to the complement control protein decay-accelerating factor (DAF) to facilitate cell entry. We present here a structure for echovirus (EV) type 12 bound to DAF using cryo-negative stain transmission electron microscopy and three-dimensional image reconstruction to 16-A resolution, which we interpreted using the atomic structures of EV11 and DAF. DAF binds to a hypervariable region of the capsid close to the 2-fold symmetry axes in an interaction that involves mostly the short consensus repeat 3 domain of DAF and the capsid protein VP2. A bulge in the density for the short consensus repeat 3 domain suggests that a loop at residues 174-180 rearranges to prevent steric collision between closely packed molecules at the 2-fold symmetry axes. Detailed analysis of receptor interactions between a variety of echoviruses and DAF using surface plasmon resonance and comparison of this structure (and our previous work; Bhella, D., Goodfellow, I. G., Roversi, P., Pettigrew, D., Chaudhry, Y., Evans, D. J., and Lea, S. M. (2004) J. Biol. Chem. 279, 8325-8332) with reconstructions published for EV7 bound to DAF support major differences in receptor recognition among these viruses. However, comparison of the electron density for the two virus.receptor complexes (rather than comparisons of the pseudo-atomic models derived from fitting the coordinates into these densities) suggests that the dramatic differences in interaction affinities/specificities may arise from relatively subtle structural differences rather than from large-scale repositioning of the receptor with respect to the virus surface.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA].
+C8I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_echovirus_25 Human echovirus 25]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C8I OCA].
 ==Reference==
@@ Line 19: / Line 18: @@
 [[Category: Protein complex]]
 [[Category: Bhella, D.]]
-[[Category: Evans, D.J.]]
+[[Category: Evans, D J.]]
 [[Category: Kerrigan, D.]]
-[[Category: Lea, S.M.]]
+[[Category: Lea, S M.]]
-[[Category: Pettigrew, D.M.]]
+[[Category: Pettigrew, D M.]]
-[[Category: Williams, D.T.]]
+[[Category: Williams, D T.]]
 [[Category: antigen]]
 [[Category: blood group antigen]]
@@ Line 43: / Line 42: @@
 [[Category: virus-receptor complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:12:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:06 2008''