1h4u: Difference between revisions
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4u RCSB], [http://www.ebi.ac.uk/pdbsum/1h4u PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4u RCSB], [http://www.ebi.ac.uk/pdbsum/1h4u PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NID1_MOUSE NID1_MOUSE]] Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 12:28, 25 December 2014
DOMAIN G2 OF MOUSE NIDOGEN-1DOMAIN G2 OF MOUSE NIDOGEN-1
Structural highlights
Function[NID1_MOUSE] Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNidogen, an invariant component of basement membranes, is a multifunctional protein that interacts with most other major basement membrane proteins. Here, we report the crystal structure of the mouse nidogen-1 G2 fragment, which contains binding sites for collagen IV and perlecan. The structure is composed of an EGF-like domain and an 11-stranded beta-barrel with a central helix. The beta-barrel domain has unexpected similarity to green fluorescent protein. A large surface patch on the beta-barrel is strikingly conserved in all metazoan nidogens. Site-directed mutagenesis demonstrates that the conserved residues are involved in perlecan binding. Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.,Hopf M, Gohring W, Ries A, Timpl R, Hohenester E Nat Struct Biol. 2001 Jul;8(7):634-40. PMID:11427896[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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