4f3j

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f3j OCA], [https://pdbe.org/4f3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f3j RCSB], [https://www.ebi.ac.uk/pdbsum/4f3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f3j ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Autosomal dominant late-onset retinal macular degeneration (L-ORMD) is caused by a single S163R mutation in the C1q and tumor necrosis factor-related protein 5 (C1QTNF5) gene. The C1QTNF5 gene encodes a secreted and membrane-associated protein involved in adhesion of retinal pigmented epithelial cells (RPE) to Bruch's membrane. The crystal structure of the trimeric globular domain of human C1QTNF5 at 1.34A resolution reveals unique features of this novel C1q family member. It lacks a Ca(2+)-binding site, displays a remarkable non-uniform distribution of surface electrostatic potentials and possesses a unique sequence (F(181)F(182)G(183)G(184)W(185)P(186)) that forms a hydrophobic plateau surrounded by Lys and Arg residues with a solvent cavity underneath. S(163) forms a hydrogen bond with F(182) in a hydrophobic area extending to the hydrophobic plateau. The pathogenic mutation S163R disrupts this hydrogen bonding and positively charges these hydrophobic areas. Thus, our analysis provides insights into the structural basis of the L-ORMD disease mechanism.

Crystal structure of the globular domain of C1QTNF5: Implications for late-onset retinal macular degeneration.,Tu X, Palczewski K J Struct Biol. 2012 Aug 7. PMID:22892318<ref>PMID:22892318</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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