2bb5

From Proteopedia

(Difference between revisions)

Current revision

Structure of Human Transcobalamin in complex with Cobalamin

Structural highlights

2bb5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

TCO2_HUMAN Defects in TCN2 are the cause of transcobalamin II deficiency (TCN2 deficiency) [MIM:275350. This results in various forms of anemia.

Function

TCO2_HUMAN Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.

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

Cobalamin (Cbl, vitamin B(12)) serves for two essential cofactors in mammals. The pathway for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors and three Cbl-transporting proteins, haptocorrin, intrinsic factor, and transcobalamin (TC). We present the structure determination of a member of the mammalian Cbl-transporter family. The crystal structures of recombinant human and bovine holo-TCs reveal a two-domain architecture, with an N-terminal alpha(6)-alpha(6) barrel and a smaller C-terminal domain. One Cbl molecule in base-on conformation is buried inside the domain interface. Structural data combined with previous binding assays indicate a domain motion in the first step of Cbl binding. In a second step, the weakly coordinated ligand H(2)O at the upper axial side of added H(2)O-Cbl is displaced by a histidine residue of the alpha(6)-alpha(6) barrel. Analysis of amino acid conservation on TC's surface in orthologous proteins suggests the location of the TC-receptor-recognition site in an extended region on the alpha(6)-alpha(6) barrel. The TC structure allows for the mapping of sites of amino acid variation due to polymorphisms of the human TC gene. Structural information is used to predict the overall fold of haptocorrin and intrinsic factor and permits a rational approach to the design of new Cbl-based bioconjugates for diagnostic or therapeutic drug delivery.

Structural basis for mammalian vitamin B12 transport by transcobalamin.,Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:16537422^[1]

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

References

↑ Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L. Structural basis for mammalian vitamin B12 transport by transcobalamin. Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:16537422

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bb5"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2bb5.png|left|200px]]
-<!--
+==Structure of Human Transcobalamin in complex with Cobalamin==
-The line below this paragraph, containing "STRUCTURE_2bb5", creates the "Structure Box" on the page.
+<StructureSection load='2bb5' size='340' side='right'caption='[[2bb5]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2bb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BB5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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=2bb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bb5 OCA], [https://pdbe.org/2bb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bb5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bb5 ProSAT]</span></td></tr>
-{{STRUCTURE_2bb5|  PDB=2bb5  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/TCO2_HUMAN TCO2_HUMAN] Defects in TCN2 are the cause of transcobalamin II deficiency (TCN2 deficiency) [MIM:[https://omim.org/entry/275350 275350]. This results in various forms of anemia.
+== Function ==
+[https://www.uniprot.org/uniprot/TCO2_HUMAN TCO2_HUMAN] Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/2bb5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bb5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cobalamin (Cbl, vitamin B(12)) serves for two essential cofactors in mammals. The pathway for its intestinal absorption, plasma transport, and cellular uptake uses cell surface receptors and three Cbl-transporting proteins, haptocorrin, intrinsic factor, and transcobalamin (TC). We present the structure determination of a member of the mammalian Cbl-transporter family. The crystal structures of recombinant human and bovine holo-TCs reveal a two-domain architecture, with an N-terminal alpha(6)-alpha(6) barrel and a smaller C-terminal domain. One Cbl molecule in base-on conformation is buried inside the domain interface. Structural data combined with previous binding assays indicate a domain motion in the first step of Cbl binding. In a second step, the weakly coordinated ligand H(2)O at the upper axial side of added H(2)O-Cbl is displaced by a histidine residue of the alpha(6)-alpha(6) barrel. Analysis of amino acid conservation on TC's surface in orthologous proteins suggests the location of the TC-receptor-recognition site in an extended region on the alpha(6)-alpha(6) barrel. The TC structure allows for the mapping of sites of amino acid variation due to polymorphisms of the human TC gene. Structural information is used to predict the overall fold of haptocorrin and intrinsic factor and permits a rational approach to the design of new Cbl-based bioconjugates for diagnostic or therapeutic drug delivery.
-===Structure of Human Transcobalamin in complex with Cobalamin===
+Structural basis for mammalian vitamin B12 transport by transcobalamin.,Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:16537422<ref>PMID:16537422</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16537422}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2bb5" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16537422 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16537422}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BB5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BB5 OCA].
-==Reference==
-Structural basis for mammalian vitamin B12 transport by transcobalamin., Wuerges J, Garau G, Geremia S, Fedosov SN, Petersen TE, Randaccio L, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4386-91. Epub 2006 Mar 14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16537422 16537422]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fedosov, S N.]]
+[[Category: Fedosov SN]]
-[[Category: Garau, G.]]
+[[Category: Garau G]]
-[[Category: Geremia, S.]]
+[[Category: Geremia S]]
-[[Category: Petersen, T E.]]
+[[Category: Petersen TE]]
-[[Category: Randaccio, L.]]
+[[Category: Randaccio L]]
-[[Category: Wuerges, J.]]
+[[Category: Wuerges J]]
-[[Category: Alpha_6 - alpha_6 barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:31:23 2008''

2bb5

From Proteopedia

Current revision

Structure of Human Transcobalamin in complex with Cobalamin

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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