1hdm: Difference between revisions

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==Overview==

The three-dimensional structure of the soluble ecto-domain of HLA-DM has, been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has, both peptide exchange activity and acts as a chaperone to peptide-free, class II MHC molecules. As predicted, the structure is similar to that of, classical class II MHC molecules except that the peptide-binding site is, altered to an almost fully closed groove. An unusual cavity is found at, the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate, both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an, inhibitor.

The three-dimensional structure of the soluble ecto-domain of HLA-DM has been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has both peptide exchange activity and acts as a chaperone to peptide-free class II MHC molecules. As predicted, the structure is similar to that of classical class II MHC molecules except that the peptide-binding site is altered to an almost fully closed groove. An unusual cavity is found at the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an inhibitor.

==Disease==

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[[Category: Protein complex]]

[[Category: Mosyak, L.]]

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

[[Category: Wiley, D C.]]

[[Category: histocompatibility protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:56:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:14 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The three-dimensional structure of the soluble ecto-domain of HLA-DM has, been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has, both peptide exchange activity and acts as a chaperone to peptide-free, class II MHC molecules. As predicted, the structure is similar to that of, classical class II MHC molecules except that the peptide-binding site is, altered to an almost fully closed groove. An unusual cavity is found at, the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate, both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an, inhibitor.
+The three-dimensional structure of the soluble ecto-domain of HLA-DM has been determined to 2.5 A resolution by X-ray crystallography. HLA-DM has both peptide exchange activity and acts as a chaperone to peptide-free class II MHC molecules. As predicted, the structure is similar to that of classical class II MHC molecules except that the peptide-binding site is altered to an almost fully closed groove. An unusual cavity is found at the center of the region that binds peptides in class II MHC molecules, and a tryptophanrich lateral surface is identified that is a candidate both for binding to HLA-DR, to effect catalysis, and to HLA-DO, an inhibitor.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Protein complex]]
 [[Category: Mosyak, L.]]
-[[Category: Wiley, D.C.]]
+[[Category: Wiley, D C.]]
 [[Category: histocompatibility protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:56:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:14 2008''