1bzq

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[[Image:1bzq.jpg|left|200px]]<br /><applet load="1bzq" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1bzq.jpg|left|200px]]
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caption="1bzq, resolution 2.8&Aring;" />
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'''COMPLEX OF A DROMEDARY SINGLE-DOMAIN VHH ANTIBODY FRAGMENT WITH RNASE A'''<br />
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{{Structure
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|PDB= 1bzq |SIZE=350|CAPTION= <scene name='initialview01'>1bzq</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5]
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|GENE=
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}}
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'''COMPLEX OF A DROMEDARY SINGLE-DOMAIN VHH ANTIBODY FRAGMENT WITH RNASE A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BZQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZQ OCA].
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1BZQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZQ OCA].
==Reference==
==Reference==
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A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops., Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L, Structure. 1999 Apr 15;7(4):361-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10196124 10196124]
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A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops., Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L, Structure. 1999 Apr 15;7(4):361-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10196124 10196124]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Camelus dromedarius]]
[[Category: Camelus dromedarius]]
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[[Category: ribonuclease]]
[[Category: ribonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:01 2008''

Revision as of 08:18, 20 March 2008


PDB ID 1bzq

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Coordinates: save as pdb, mmCIF, xml



COMPLEX OF A DROMEDARY SINGLE-DOMAIN VHH ANTIBODY FRAGMENT WITH RNASE A


Overview

BACKGROUND: Camelid serum contains a large fraction of functional heavy-chain antibodies - homodimers of heavy chains without light chains. The variable domains of these heavy-chain antibodies (VHH) have a long complementarity determining region 3 (CDR3) loop that compensates for the absence of the antigen-binding loops of the variable light chains (VL). In the case of the VHH fragment cAb-Lys3, part of the 24 amino acid long CDR3 loop protrudes from the antigen-binding surface and inserts into the active-site cleft of its antigen, rendering cAb-Lys3 a competitive enzyme inhibitor. RESULTS: A dromedary VHH with specificity for bovine RNase A, cAb-RN05, has a short CDR3 loop of 12 amino acids and is not a competitive enzyme inhibitor. The structure of the cAb-RN05-RNase A complex has been solved at 2.8 A. The VHH scaffold architecture is close to that of a human VH (variable heavy chain). The structure of the antigen-binding hypervariable 1 loop (H1) of both cAb-RN05 and cAb-Lys3 differ from the known canonical structures; in addition these H1 loops resemble each other. The CDR3 provides an antigen-binding surface and shields the face of the domain that interacts with VL in conventional antibodies. CONCLUSIONS: VHHs adopt the common immunoglobulin fold of variable domains, but the antigen-binding loops deviate from the predicted canonical structure. We define a new canonical structure for the H1 loop of immunoglobulins, with cAb-RN05 and cAb-Lys3 as reference structures. This new loop structure might also occur in human or mouse VH domains. Surprisingly, only two loops are involved in antigen recognition; the CDR2 does not participate. Nevertheless, the antigen binding occurs with nanomolar affinities because of a preferential usage of mainchain atoms for antigen interaction.

About this Structure

1BZQ is a Single protein structure of sequence from Bos taurus and Camelus dromedarius. Full crystallographic information is available from OCA.

Reference

A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops., Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, Wyns L, Structure. 1999 Apr 15;7(4):361-70. PMID:10196124

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