2uv3: Difference between revisions

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==Overview==

Signal regulatory protein (SIRP) alpha is a membrane receptor that sends, inhibitory signals to myeloid cells by engagement of CD47. The high, resolution x-ray structure of the N-terminal ligand binding domain shows, it to have a distinctive immunoglobulin superfamily V-like fold., Site-directed mutagenesis suggests that CD47 is bound at a surface, involving the BC, FG, and DE loops, which distinguishes it from other, immunoglobulin superfamily surface proteins that use the faces of the, fold, but resembles antigen receptors. The SIRP interaction is confined to, a single domain, and its use of an extended DE loop strengthens the, similarity with T cell receptor binding and the suggestion that they are, closely related in evolution. The employment of loops to form the, CD47-binding surface provides a mechanism for small sequence changes to, modulate binding specificity, explaining the different binding properties, of SIRP family members.

Signal regulatory protein (SIRP) alpha is a membrane receptor that sends inhibitory signals to myeloid cells by engagement of CD47. The high resolution x-ray structure of the N-terminal ligand binding domain shows it to have a distinctive immunoglobulin superfamily V-like fold. Site-directed mutagenesis suggests that CD47 is bound at a surface involving the BC, FG, and DE loops, which distinguishes it from other immunoglobulin superfamily surface proteins that use the faces of the fold, but resembles antigen receptors. The SIRP interaction is confined to a single domain, and its use of an extended DE loop strengthens the similarity with T cell receptor binding and the suggestion that they are closely related in evolution. The employment of loops to form the CD47-binding surface provides a mechanism for small sequence changes to modulate binding specificity, explaining the different binding properties of SIRP family members.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Barclay, A.N.]]

[[Category: Barclay, A N.]]

[[Category: Dunlop, D.C.]]

[[Category: Dunlop, D C.]]

[[Category: Harlos, K.]]

[[Category: Hatherley, D.]]

[[Category: Stuart, D.I.]]

[[Category: Stuart, D I.]]

[[Category: MES]]

[[Category: SO4]]

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[[Category: transmembrane]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:33 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Signal regulatory protein (SIRP) alpha is a membrane receptor that sends, inhibitory signals to myeloid cells by engagement of CD47. The high, resolution x-ray structure of the N-terminal ligand binding domain shows, it to have a distinctive immunoglobulin superfamily V-like fold., Site-directed mutagenesis suggests that CD47 is bound at a surface, involving the BC, FG, and DE loops, which distinguishes it from other, immunoglobulin superfamily surface proteins that use the faces of the, fold, but resembles antigen receptors. The SIRP interaction is confined to, a single domain, and its use of an extended DE loop strengthens the, similarity with T cell receptor binding and the suggestion that they are, closely related in evolution. The employment of loops to form the, CD47-binding surface provides a mechanism for small sequence changes to, modulate binding specificity, explaining the different binding properties, of SIRP family members.
+Signal regulatory protein (SIRP) alpha is a membrane receptor that sends inhibitory signals to myeloid cells by engagement of CD47. The high resolution x-ray structure of the N-terminal ligand binding domain shows it to have a distinctive immunoglobulin superfamily V-like fold. Site-directed mutagenesis suggests that CD47 is bound at a surface involving the BC, FG, and DE loops, which distinguishes it from other immunoglobulin superfamily surface proteins that use the faces of the fold, but resembles antigen receptors. The SIRP interaction is confined to a single domain, and its use of an extended DE loop strengthens the similarity with T cell receptor binding and the suggestion that they are closely related in evolution. The employment of loops to form the CD47-binding surface provides a mechanism for small sequence changes to modulate binding specificity, explaining the different binding properties of SIRP family members.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Barclay, A.N.]]
+[[Category: Barclay, A N.]]
-[[Category: Dunlop, D.C.]]
+[[Category: Dunlop, D C.]]
 [[Category: Harlos, K.]]
 [[Category: Hatherley, D.]]
-[[Category: Stuart, D.I.]]
+[[Category: Stuart, D I.]]
 [[Category: MES]]
 [[Category: SO4]]
@@ Line 33: / Line 33: @@
 [[Category: transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:47:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:50:33 2008''