1b4f: Difference between revisions

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==Overview==

The sterile alpha motif (SAM) domain is a protein interaction module that, is present in diverse signal-transducing proteins. SAM domains are known, to form homo- and hetero-oligomers. The crystal structure of the SAM, domain from an Eph receptor tyrosine kinase, EphB2, reveals two large, interfaces. In one interface, adjacent monomers exchange amino-terminal, peptides that insert into a hydrophobic groove on each neighbor. A second, interface is composed of the carboxyl-terminal helix and a nearby loop. A, possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.

The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.

==Disease==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Bowie, J.U.]]

[[Category: Bowie, J U.]]

[[Category: Goodwill, K.E.]]

[[Category: Goodwill, K E.]]

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

[[Category: Thanos, C D.]]

[[Category: eph receptor]]

[[Category: oligomer]]

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[[Category: signal transduction]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The sterile alpha motif (SAM) domain is a protein interaction module that, is present in diverse signal-transducing proteins. SAM domains are known, to form homo- and hetero-oligomers. The crystal structure of the SAM, domain from an Eph receptor tyrosine kinase, EphB2, reveals two large, interfaces. In one interface, adjacent monomers exchange amino-terminal, peptides that insert into a hydrophobic groove on each neighbor. A second, interface is composed of the carboxyl-terminal helix and a nearby loop. A, possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.
+The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.
 ==Disease==
@@ Line 16: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Bowie, J.U.]]
+[[Category: Bowie, J U.]]
-[[Category: Goodwill, K.E.]]
+[[Category: Goodwill, K E.]]
-[[Category: Thanos, C.D.]]
+[[Category: Thanos, C D.]]
 [[Category: eph receptor]]
 [[Category: oligomer]]
@@ Line 24: / Line 24: @@
 [[Category: signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:30:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:21 2008''