1gl4: Difference between revisions

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==Overview==

Nidogen and perlecan are large multifunctional basement membrane (BM), proteins conserved in all metazoa. Their high-affinity interaction, which, is likely to contribute to BM assembly and function, is mediated by the, central G2 domain in nidogen and the third immunoglobulin (IG)-like domain, in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution, of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to, the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2, beta-barrel using beta-strands C, D and F. Nidogen-1 residues, participating in the extensive interface are highly conserved, whereas the, corresponding binding site on perlecan is more variable. We hypothesize, that a second, as yet unidentified, activity of nidogen overlaps with, perlecan binding and accounts for the unusually high degree of surface, conservation in the G2 domain.

Nidogen and perlecan are large multifunctional basement membrane (BM) proteins conserved in all metazoa. Their high-affinity interaction, which is likely to contribute to BM assembly and function, is mediated by the central G2 domain in nidogen and the third immunoglobulin (IG)-like domain in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2 beta-barrel using beta-strands C, D and F. Nidogen-1 residues participating in the extensive interface are highly conserved, whereas the corresponding binding site on perlecan is more variable. We hypothesize that a second, as yet unidentified, activity of nidogen overlaps with perlecan binding and accounts for the unusually high degree of surface conservation in the G2 domain.

==About this Structure==

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[[Category: proteoglycan]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Nidogen and perlecan are large multifunctional basement membrane (BM), proteins conserved in all metazoa. Their high-affinity interaction, which, is likely to contribute to BM assembly and function, is mediated by the, central G2 domain in nidogen and the third immunoglobulin (IG)-like domain, in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution, of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to, the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2, beta-barrel using beta-strands C, D and F. Nidogen-1 residues, participating in the extensive interface are highly conserved, whereas the, corresponding binding site on perlecan is more variable. We hypothesize, that a second, as yet unidentified, activity of nidogen overlaps with, perlecan binding and accounts for the unusually high degree of surface, conservation in the G2 domain.
+Nidogen and perlecan are large multifunctional basement membrane (BM) proteins conserved in all metazoa. Their high-affinity interaction, which is likely to contribute to BM assembly and function, is mediated by the central G2 domain in nidogen and the third immunoglobulin (IG)-like domain in perlecan, IG3. We have solved the crystal structure at 2.0 A resolution of the mouse nidogen-1 G2-perlecan IG3 complex. Perlecan IG3 belongs to the I-set of the IG superfamily and binds to the wall of the nidogen-1 G2 beta-barrel using beta-strands C, D and F. Nidogen-1 residues participating in the extensive interface are highly conserved, whereas the corresponding binding site on perlecan is more variable. We hypothesize that a second, as yet unidentified, activity of nidogen overlaps with perlecan binding and accounts for the unusually high degree of surface conservation in the G2 domain.
 ==About this Structure==
@@ Line 26: / Line 26: @@
 [[Category: proteoglycan]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:40:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:20 2008''