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1p4l

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Revision as of 15:35, 25 December 2014

Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb

Structural highlights

1p4l is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1p1z, 1vac, 1qo3
Gene:	H2-K (Mus musculus), B2M (Mus musculus), KLRA3 OR LY49C OR LY-49C (Mus musculus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[KLRA3_MOUSE] Receptor on natural killer (NK) cells for class I MHC.^[1] [HA1B_MOUSE] Involved in the presentation of foreign antigens to the immune system. [OVAL_CHICK] Non-inhibitory serpin. Storage protein of egg white.^[2] ^[3] [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.

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 PubMed

The Ly49 family of natural killer (NK) receptors regulates NK cell function by sensing major histocompatibility complex (MHC) class I. Ly49 receptors show complex patterns of MHC class I cross-reactivity and, in certain cases, peptide selectivity. To investigate whether specificity differences result from topological differences in MHC class I engagement, we determined the structure of the peptide-selective receptor Ly49C in complex with H-2K(b). The Ly49C homodimer binds two MHC class I molecules in symmetrical way, a mode distinct from that of Ly49A, which binds MHC class I asymmetrically. Ly49C does not directly contact the MHC-bound peptide. In addition, MHC crosslinking by Ly49C was demonstrated in solution. We propose a dynamic model for Ly49-MHC class I interactions involving conformational changes in the receptor, whereby variations in Ly49 dimerization mediate different MHC-binding modes.

Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b).,Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brennan J, Lemieux S, Freeman JD, Mager DL, Takei F. Heterogeneity among Ly-49C natural killer (NK) cells: characterization of highly related receptors with differing functions and expression patterns. J Exp Med. 1996 Dec 1;184(6):2085-90. PMID:8976165
↑ Meek RL, Walsh KA, Palmiter RD. The signal sequence of ovalbumin is located near the NH2 terminus. J Biol Chem. 1982 Oct 25;257(20):12245-51. PMID:6749856
↑ Robinson A, Meredith C, Austen BM. Isolation and properties of the signal region from ovalbumin. FEBS Lett. 1986 Jul 28;203(2):243-6. PMID:3732511
↑ Dam J, Guan R, Natarajan K, Dimasi N, Chlewicki LK, Kranz DM, Schuck P, Margulies DH, Mariuzza RA. Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b). Nat Immunol. 2003 Dec;4(12):1213-22. Epub 2003 Nov 2. PMID:14595439 doi:10.1038/ni1006

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p4l"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1p4l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P4L FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p1z|1p1z]], [[1vac|1vac]], [[1qo3|1qo3]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p1z|1p1z]], [[1vac|1vac]], [[1qo3|1qo3]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), KLRA3 OR LY49C OR LY-49C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2-K ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), KLRA3 OR LY49C OR LY-49C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p4l RCSB], [http://www.ebi.ac.uk/pdbsum/1p4l PDBsum]</span></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=1p4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p4l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p4l RCSB], [http://www.ebi.ac.uk/pdbsum/1p4l PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/KLRA3_MOUSE KLRA3_MOUSE]] Receptor on natural killer (NK) cells for class I MHC.<ref>PMID:8976165</ref>  [[http://www.uniprot.org/uniprot/HA1B_MOUSE HA1B_MOUSE]] Involved in the presentation of foreign antigens to the immune system. [[http://www.uniprot.org/uniprot/OVAL_CHICK OVAL_CHICK]] Non-inhibitory serpin. Storage protein of egg white.<ref>PMID:6749856</ref> <ref>PMID:3732511</ref>  [[http://www.uniprot.org/uniprot/B2MG_MOUSE B2MG_MOUSE]] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 </StructureSection>
 [[Category: Mus musculus]]
-[[Category: Dam, J.]]
+[[Category: Dam, J]]
-[[Category: Dimasi, N.]]
+[[Category: Dimasi, N]]
-[[Category: Guan, R.]]
+[[Category: Guan, R]]
-[[Category: Mariuzza, R A.]]
+[[Category: Mariuzza, R A]]
-[[Category: Natarajan, K.]]
+[[Category: Natarajan, K]]
 [[Category: C-type lectin-like domain]]
 [[Category: Immune system]]
 [[Category: Mhc class i]]
 [[Category: Natural killer receptor]]

1p4l

From Proteopedia

Revision as of 15:35, 25 December 2014

Crystal structure of NK receptor Ly49C mutant with its MHC class I ligand H-2Kb

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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